EC number:2.7.9.1
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.7 Transferring phosphorus-containing groups |
| 2.7.9 Phosphotransferases with paired acceptors |
| ID: | 2.7.9.1 | ||
|---|---|---|---|
| Description: | Pyruvate, phosphate dikinase. | ||
| Alternative Name: |
Pyruvate,phosphate dikinase. Pyruvate,orthophosphate dikinase. PPDK. | ||
| Prosite: | PDOC00527; | ||
| PDB: |
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| Cath: | 1.10.189.10; 3.20.20.60; 3.30.1490.20; 3.30.470.20; 3.50.30.10; 1.20.80.30; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.7.9.1 |
| BRENDA Enzyme Link: | BRENDA 2.7.9.1 |
| KEGG Enzyme Link: | KEGG2.7.9.1 |
| BioCyc Enzyme Link: | BioCyc 2.7.9.1 |
| ExPASy Enzyme Link: | ExPASy2.7.9.1 |
| EC2PDB Enzyme Link: | EC2PDB 2.7.9.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.7.9.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.7.9.1 |
| IntEnz Enzyme Link: | IntEnz 2.7.9.1 |
| MEDLINE Enzyme Link: | MEDLINE 2.7.9.1 |
| RHEA:43688 | N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] + pyruvate = L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] + phosphoenolpyruvate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[CH3;+0:3])=[O;H0;+0:4].[*:5]:[n;H0;+0:6](:[*:7])-[P;H0;+0:8](=[*:9])(-[*:10])-[*:11]>>[*:5]:[nH;+0:6]:[*:7].[*:9]=[P;H0;+0:8](-[*:10])(-[*:11])-[O;H0;+0:4]-[C;H0;+0:2](-[*:1])=[CH2;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Regulation of C4 photosynthesis: identification of a catalytically important histidine residue and its role in the regulation of pyruvate,Pi dikinase. | Burnell JN, Hatch MD | 1984 May 15 | 6326674 |
| Studies on the mechanism of activation and inactivation of pyruvate, phosphate dikinase. A possible regulatory role for the enzyme in the C4 dicarboxylic acid pathway of photosynthesis. | Hatch MD, Slack CR | 1969 May | 5821721 |
| Cloning and characterization of Escherichia coli DUF299: a bifunctional ADP-dependent kinase--Pi-dependent pyrophosphorylase from bacteria. | Burnell JN | 2010 Jan 3 | 20044937 |
| RHEA:43684 | ATP + L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] + phosphate = AMP + diphosphate + H(+) + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] |
| RULE(radius=1) | [*:1]-[O;H0;+0:2]-[P;H0;+0:3](-[*:4])(=[*:5])-[*:6].[*:7]:[nH;+0:8]:[*:9].[*:10]=[P;H0;+0:11](-[*:12])(-[*:13])-[OH;+0:14]>>[*:1]-[OH;+0:2].[*:4]-[P;H0;+0:3](=[*:5])(-[*:6])-[OH;+0:14].[*:7]:[n;H0;+0:8](:[*:9])-[P;H0;+0:11](=[*:10])(-[*:12])-[*:13] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Regulation of C4 photosynthesis: identification of a catalytically important histidine residue and its role in the regulation of pyruvate,Pi dikinase. | Burnell JN, Hatch MD | 1984 May 15 | 6326674 |
| Studies on the mechanism of activation and inactivation of pyruvate, phosphate dikinase. A possible regulatory role for the enzyme in the C4 dicarboxylic acid pathway of photosynthesis. | Hatch MD, Slack CR | 1969 May | 5821721 |
| Cloning and characterization of Escherichia coli DUF299: a bifunctional ADP-dependent kinase--Pi-dependent pyrophosphorylase from bacteria. | Burnell JN | 2010 Jan 3 | 20044937 |
| Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory protein gene. | Burnell JN, Chastain CJ | 2006 Jun 30 | 16696949 |
| RHEA:10756 | ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[CH3;+0:3])=[O;H0;+0:4].[*:5]-[O;H0;+0:6]-[P;H0;+0:7](-[*:8])(=[*:9])-[*:10].[*:11]=[P;H0;+0:12](-[*:13])(-[*:14])-[OH;+0:15]>>[*:1]-[C;H0;+0:2](=[CH2;+0:3])-[O;H0;+0:4]-[P;H0;+0:12](=[*:11])(-[*:13])-[*:14].[*:5]-[OH;+0:6].[*:8]-[P;H0;+0:7](=[*:9])(-[*:10])-[OH;+0:15] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Increased pyruvate orthophosphate dikinase activity results in an alternative gluconeogenic pathway in Rhizobium (Sinorhizobium) meliloti. | Osterås M, Driscoll BT, Finan TM | 1997 May | 9168612 |
| Substrate binding domains in pyruvate phosphate dikinase. | Carroll LJ, Xu Y, Thrall SH, Martin BM, Dunaway-Mariano D | 1994 Feb 8 | 8110745 |
| Location of the catalytic site for phosphoenolpyruvate formation within the primary structure of Clostridium symbiosum pyruvate phosphate dikinase. 1. Identification of an essential cysteine by chemical modification with [1-14C]bromopyruvate and site-directed mutagenesis. | Xu Y, Yankie L, Shen L, Jung YS, Mariano PS, Dunaway-Mariano D, Martin BM | 1995 Feb 21 | 7857929 |
| The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis are both bifunctional and interact with the catalytic and nucleotide-binding domains of pyruvate, orthophosphate dikinase. | Astley HM, Parsley K, Aubry S, Chastain CJ, Burnell JN, Webb ME, Hibberd JM | 2011 Dec | 21883547 |
| Functional evolution of C(4) pyruvate, orthophosphate dikinase. | Chastain CJ, Failing CJ, Manandhar L, Zimmerman MA, Lakner MM, Nguyen TH | 2011 May | 21414960 |