UniProt functional annotation for P11155



	UniProt functional annotation for P11155

UniProt code: P11155.

Organism: Zea mays (Maize).

Taxonomy: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.

Function: Formation of phosphoenolpyruvate, which is the primary acceptor of CO(2) in C4 and some Crassulacean acid metabolism plants. {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:21414960}.

Catalytic activity: Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1; Evidence={ECO:0000269|PubMed:10683263, ECO:0000269|PubMed:21414960, ECO:0000269|PubMed:9038349};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15667207, ECO:0000305|PubMed:9287137};

Activity regulation: Activated by light-induced dephosphorylation. Inhibited by dark-induced phosphorylation. Both reactions are catalyzed by PDRP1. Inactivated by cold due to the dissociation of the homotetramer. Independent of circadian regulation (PubMed:24710069). {ECO:0000269|PubMed:10683263, ECO:0000269|PubMed:16660615, ECO:0000269|PubMed:24710069, ECO:0000269|PubMed:9038349}.

Biophysicochemical properties: Kinetic parameters: KM=158 uM for pyruvate {ECO:0000269|PubMed:9038349}; KM=178 uM for pyruvate {ECO:0000269|PubMed:21414960}; KM=95 uM for ATP {ECO:0000269|PubMed:9038349}; KM=194 uM for phosphoenolpyruvate {ECO:0000269|PubMed:21414960}; KM=408 uM for phosphate {ECO:0000269|PubMed:9038349}; Temperature dependence: Loss of activity below 10 degrees Celsius. {ECO:0000269|PubMed:9038349};

Pathway: Photosynthesis; C4 acid pathway.

Subunit: Homotetramer. {ECO:0000269|PubMed:15667207}.

Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:22833285}. Cytoplasm {ECO:0000269|PubMed:1668653}. Note=Isoform C4PPDKZM1 is targeted to the chloroplast while isoform CYPPDKZM1 is found in the cytoplasm. Can be found associated with the thylakoid membrane.

Tissue specificity: Isoform C4PPDKZM1 mainly localized in mesophyll cells and only a low level is found in bundle sheath cells. Isoform CYPPDKZM1 expressed in roots, stems and etiolated leaves. {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:2158100, ECO:0000269|PubMed:24710069}.

Induction: Isoform C4ppdkZm1 is light-inducible. {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:24710069}.

Domain: The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.

Ptm: Phosphorylation of Thr-527 in the dark inactivates the enzyme, dephosphorylation upon light stimulation reactivates the enzyme (PubMed:2834385). More highly phosphorylated when grown under high rather than low light regimes (70 vs 900 umol photons/m-2/s). the degree of phosphorylation is strictly regulated by light intensity and the light/dark transition has no influence (PubMed:24710069). Phosphorylated in both mesophyll and bundle sheath cells (PubMed:22833285). The phosphorylation at Ser-528 may be important for the phosphorylation at Thr-527 and may also be regulated by light intensity (PubMed:24710069). {ECO:0000269|PubMed:22833285, ECO:0000269|PubMed:24710069, ECO:0000269|PubMed:2834385}.

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.

Miscellaneous: PubMed:1668653 shows the existence of a second gene coding only for the short cytoplasmic isoform of PPDK.

Miscellaneous: [Isoform CYPPDKZM1]: Produced by alternative promoter usage (PubMed:1668653). Cytoplasmic (PubMed:1668653). Initiator Met-1 is removed (PubMed:24710069). {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:24710069}.

Similarity: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.

Sequence caution: Sequence=AAA33495.1; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Zea mays (Maize).
Taxonomy:		Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.



Function:		Formation of phosphoenolpyruvate, which is the primary acceptor of CO(2) in C4 and some Crassulacean acid metabolism plants. {ECO:0000269\|PubMed:1668653, ECO:0000269\|PubMed:21414960}.


Catalytic activity:		Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1; Evidence={ECO:0000269\|PubMed:10683263, ECO:0000269\|PubMed:21414960, ECO:0000269\|PubMed:9038349};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:15667207, ECO:0000305\|PubMed:9287137};
Activity regulation:		Activated by light-induced dephosphorylation. Inhibited by dark-induced phosphorylation. Both reactions are catalyzed by PDRP1. Inactivated by cold due to the dissociation of the homotetramer. Independent of circadian regulation (PubMed:24710069). {ECO:0000269\|PubMed:10683263, ECO:0000269\|PubMed:16660615, ECO:0000269\|PubMed:24710069, ECO:0000269\|PubMed:9038349}.
Biophysicochemical properties:		Kinetic parameters: KM=158 uM for pyruvate {ECO:0000269\|PubMed:9038349}; KM=178 uM for pyruvate {ECO:0000269\|PubMed:21414960}; KM=95 uM for ATP {ECO:0000269\|PubMed:9038349}; KM=194 uM for phosphoenolpyruvate {ECO:0000269\|PubMed:21414960}; KM=408 uM for phosphate {ECO:0000269\|PubMed:9038349}; Temperature dependence: Loss of activity below 10 degrees Celsius. {ECO:0000269\|PubMed:9038349};
Pathway:		Photosynthesis; C4 acid pathway.
Subunit:		Homotetramer. {ECO:0000269\|PubMed:15667207}.
Subcellular location:		Plastid, chloroplast {ECO:0000269\|PubMed:1668653, ECO:0000269\|PubMed:22833285}. Cytoplasm {ECO:0000269\|PubMed:1668653}. Note=Isoform C4PPDKZM1 is targeted to the chloroplast while isoform CYPPDKZM1 is found in the cytoplasm. Can be found associated with the thylakoid membrane.
Tissue specificity:		Isoform C4PPDKZM1 mainly localized in mesophyll cells and only a low level is found in bundle sheath cells. Isoform CYPPDKZM1 expressed in roots, stems and etiolated leaves. {ECO:0000269\|PubMed:1668653, ECO:0000269\|PubMed:2158100, ECO:0000269\|PubMed:24710069}.
Induction:		Isoform C4ppdkZm1 is light-inducible. {ECO:0000269\|PubMed:1668653, ECO:0000269\|PubMed:24710069}.
Domain:		The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Ptm:		Phosphorylation of Thr-527 in the dark inactivates the enzyme, dephosphorylation upon light stimulation reactivates the enzyme (PubMed:2834385). More highly phosphorylated when grown under high rather than low light regimes (70 vs 900 umol photons/m-2/s). the degree of phosphorylation is strictly regulated by light intensity and the light/dark transition has no influence (PubMed:24710069). Phosphorylated in both mesophyll and bundle sheath cells (PubMed:22833285). The phosphorylation at Ser-528 may be important for the phosphorylation at Thr-527 and may also be regulated by light intensity (PubMed:24710069). {ECO:0000269\|PubMed:22833285, ECO:0000269\|PubMed:24710069, ECO:0000269\|PubMed:2834385}.
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.
Miscellaneous:		PubMed:1668653 shows the existence of a second gene coding only for the short cytoplasmic isoform of PPDK.
Miscellaneous:		[Isoform CYPPDKZM1]: Produced by alternative promoter usage (PubMed:1668653). Cytoplasmic (PubMed:1668653). Initiator Met-1 is removed (PubMed:24710069). {ECO:0000269\|PubMed:1668653, ECO:0000269\|PubMed:24710069}.
Similarity:		Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
Sequence caution:		Sequence=AAA33495.1; Type=Frameshift; Evidence={ECO:0000305};