Enzyme

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EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.2 Phosphotransferases with a carboxy group as acceptor
ID:2.7.2.15
Description:Propionate kinase.
Alternative Name: Propionate/acetate kinase.
Prosite: PDOC00826;
PDB:
PDBScop
Cath: 3.30.420.40;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.2.15
BRENDA Enzyme Link: BRENDA 2.7.2.15
KEGG Enzyme Link: KEGG2.7.2.15
BioCyc Enzyme Link: BioCyc 2.7.2.15
ExPASy Enzyme Link: ExPASy2.7.2.15
EC2PDB Enzyme Link: EC2PDB 2.7.2.15
ExplorEnz Enzyme Link: ExplorEnz 2.7.2.15
PRIAM enzyme-specific profiles Link: PRIAM 2.7.2.15
IntEnz Enzyme Link: IntEnz 2.7.2.15
MEDLINE Enzyme Link: MEDLINE 2.7.2.15
MSA:

2.7.2.15;

Phylogenetic Tree:

2.7.2.15;

Uniprot:
M-CSA:
RHEA:23148 ATP + propanoate = ADP + propanoyl phosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate.Hesslinger C, Fairhurst SA, Sawers G1998 Jan9484901
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium.Simanshu DK, Murthy MR2005 Jan 116508089
Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily.Simanshu DK, Savithri HS, Murthy MR2005 Sep 3016139298
Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and propionate catabolic pathways needed for expression of the prpBCDE operon during growth of Salmonella enterica on 1,2-propanediol.Palacios S, Starai VJ, Escalante-Semerena JC2003 May12700259