9CAUD:A0A0K2D0M2

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	ECO:0000247		PMID:12538896 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
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References

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