8CJ5

Arabidopsis thaliana Phosphoenolpyruvate carboxylase PPC1 A651V mutant with bound phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008964	molecular_function	phosphoenolpyruvate carboxylase activity
A	0015977	biological_process	carbon fixation
A	0015979	biological_process	photosynthesis
A	0016036	biological_process	cellular response to phosphate starvation
A	0016829	molecular_function	lyase activity
A	0048046	cellular_component	apoplast
A	0048366	biological_process	leaf development
A	0051262	biological_process	protein tetramerization
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008964	molecular_function	phosphoenolpyruvate carboxylase activity
B	0015977	biological_process	carbon fixation
B	0015979	biological_process	photosynthesis
B	0016036	biological_process	cellular response to phosphate starvation
B	0016829	molecular_function	lyase activity
B	0048046	cellular_component	apoplast
B	0048366	biological_process	leaf development
B	0051262	biological_process	protein tetramerization

Functional Information from PROSITE/UniProt

site_id	PS00393
Number of Residues	13
Details	PEPCASE_2 Phosphoenolpyruvate carboxylase active site 2. VMIGYSDSgKDAG

Chain	Residue	Details
A	VAL593-GLY605

site_id	PS00781
Number of Residues	12
Details	PEPCASE_1 Phosphoenolpyruvate carboxylase active site 1. VlTAHPTQsvRR

Chain	Residue	Details
A	VAL169-ARG180

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:19228119, ECO:0007744\|PubMed:18433157, ECO:0007744\|PubMed:19245862, ECO:0007744\|PubMed:19376835

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18433157