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9CAUD:A0A0K2D0M2

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Species (Taxon ID) Bacillus phage TsarBomba. (1690456)
Gene Name(s) No Information Provided.
Protein Name(s) Dephospho-CoA kinase (ECO:0000313 with EMBL:ALA13146.1)
External Links
UniProt A0A0K2D0M2
EMBL KT224359
RefSeq YP_009206865.1
GeneID 26633356
GO GO:0016301
Gene3D 3.40.50.300
InterPro IPR027417
SUPFAM SSF52540

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

Contributes to

GO:0016301

kinase activity

PMID:12538896[1]

ECO:0000247

PMID:12538896[1] UniProtKB:A0A0K2D0M2


F

This enzyme forms a tightly packed trimer in its crystal state, in contrast to its observed monomeric structure in solution and to the monomeric, homologous DPCK structure from Haemophilus influenzae. We have confirmed the existence of the trimeric form of the enzyme in solution using gel filtration chromatography measurements. Dephospho-CoA kinase is structurally similar to many nucleoside kinases and other P-loop-containing nucleotide triphosphate hydrolases, despite having negligible sequence similarity to these enzymes. Each monomer consists of five parallel beta-strands flanked by alpha-helices, with an ATP-binding site formed by a P-loop motif. Orthologs of the E. coli DPCK sequence exist in a wide range of organisms, including humans. Multiple alignment of orthologous DPCK sequences reveals a set of highly conserved residues in the vicinity of the nucleotide/CoA binding site.

The locations of residues conserved among orthologous DPCK sequences correspond to parts of the structure expected to be involved in catalysis, based on the well-characterized behavior of similar proteins.Sequence alignment of E. coli, S. cerevisiae, A. thaliana, C. elegans, D. melanogaster, and human DPCK sequences (Fig. 6 ▶) shows conservation of residues, as identified above, which are involved in catalysis for the E. coli enzyme. Most of the strictly conserved residues involved in nucleotide binding for bacterial species (e.g., the P-loop residues and the E. coli Arg-140 residue) are also conserved among the eukaryotic sequences. Note, however, that for some conserved bacterial residues suggested to be involved in CoA binding, such as Pro-113 and Leu-114, strict residue conservation among the eukaryotic sequences is absent due to mutations among the bifunctional PPAT/DPCK sequences, perhaps hinting at modified mechanisms of CoA binding in such enzymes.

complete
CACAO 11452

enables

GO:0016301

kinase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

Notes

References

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  1. 1.0 1.1 O'Toole, N et al. (2003) Crystal structure of a trimeric form of dephosphocoenzyme A kinase from Escherichia coli. Protein Sci. 12 327-36 PubMed GONUTS page