|
|
||
|
|
|
|
|
UniProt functional annotation for P08839 | ||
|
|
|
|
|
|
||
| UniProt code: P08839. |
|
||
| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
|
||
|
||
| Function: | |
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) (PubMed:7876255, PubMed:12705838, PubMed:17053069). Can also use (Z)-3-fluoro-PEP (ZFPEP), (Z)-3-methyl- PEP (ZMePEP), (Z)-3-chloro-PEP (ZClPEP) and (E)-3-chloro-PEP (EClPEP) as alternative phosphoryl donors (PubMed:12705838). {ECO:0000269|PubMed:12705838, ECO:0000269|PubMed:17053069, ECO:0000269|PubMed:7876255}. |
|
||
| Catalytic activity: | |
Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho- L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA- COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979, ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9; Evidence={ECO:0000269|PubMed:12705838}; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17053069}; |
| Activity regulation: | |
Inhibited by oxalate. {ECO:0000269|PubMed:12705838}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.11 mM for ZFPEP {ECO:0000269|PubMed:12705838}; KM=0.12 mM for EClPEP {ECO:0000269|PubMed:12705838}; KM=0.14 mM for PEP {ECO:0000269|PubMed:12705838}; KM=0.25 mM for ZClPEP {ECO:0000269|PubMed:12705838}; KM=0.43 mM for ZMePEP {ECO:0000269|PubMed:12705838}; Note=Kcat is 3830 min(-1) with PEP as substrate. Kcat is 370 min(-1) with ZFPEP as substrate. Kcat is 285 min(-1) with ZMePEP as substrate. Kcat is 15.8 min(-1) with ZClPEP as substrate. Kcat is 2.8 min(-1) with EClPEP as substrate. {ECO:0000269|PubMed:12705838}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:12705838, ECO:0000269|PubMed:17053069}. |
| Subcellular location: | |
Cytoplasm {ECO:0000305}. |
| Domain: | |
The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site. {ECO:0000269|PubMed:17053069}. |
| Miscellaneous: | |
The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain. {ECO:0000269|PubMed:17053069}. |
| Miscellaneous: | |
Enzyme I of the sugar PTS has been shown to phosphorylate NPr of the nitrogen-metabolic PTS, though much less efficiently than it does HPr. This process may link carbon and nitrogen assimilation. {ECO:0000269|PubMed:7876255}. |
| Similarity: | |
Belongs to the PEP-utilizing enzyme family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.