1QB4

CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1qb4a_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Phosphoenolpyruvate/pyruvate domain	Phosphoenolpyruvate carboxylase	Phosphoenolpyruvate carboxylase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Phosphoenolpyruvate/pyruvate domain	8042667	3000510	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PEPcase	e1qb4A1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PEPcase	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00311	Phosphoenolpyruvate carboxylase (PEPcase)	Phosphoenolpyruvate carboxylase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PHOSPHOENOLPYRUVATE CARBOXYLASE	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding phosphoenolpyruvate carboxylase activity phosphoenolpyruvate carboxykinase activity carboxy-lyase activity lyase activity catalytic activity carbon-carbon lyase activity identical protein binding protein binding	aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds cellular metabolic process metabolic process cellular process primary metabolic process generation of precursor metabolites and energy organic substance metabolic process carbon fixation monosaccharide metabolic process carbohydrate metabolic process small molecule biosynthetic process aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds cellular metabolic process metabolic process cellular process primary metabolic process generation of precursor metabolites and energy organic substance metabolic process carbon fixation monosaccharide metabolic process carbohydrate metabolic process small molecule biosynthetic process carbohydrate biosynthetic process hexose metabolic process monosaccharide biosynthetic process gluconeogenesis hexose biosynthetic process biosynthetic process organic substance biosynthetic process small molecule metabolic process glucose metabolic process protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular component organization or biogenesis oxoacid metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process organic acid metabolic process oxaloacetate metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR015813	Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily	Homologous Superfamily
A	IPR021135	Phosphoenolpyruvate carboxylase	Family
A	IPR033129	Phosphoenolpyruvate carboxylase, His active site	Active Site
A	IPR018129	Phosphoenolpyruvate carboxylase, Lys active site	Active Site
A	IPR022805	Phosphoenolpyruvate carboxylase, bacterial/plant-type	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	phosphoenolpyruvate carboxylase M-CSA #857	Phosphoenolpyruvate carboxylase (PEPC) catalyses the irreversible carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA) and Pi using divalent Mg(II) or Mn(II) as a cofactor. The active species for initial carboxylation is not carbon dioxide but the chemically less reactive bicarbonate anion, which dominates in the cytoplasm where PEPC functions. The enzyme is present in all photosynthetic organisms, including higher plants, green algae, cyanobacteria and photosynthetic bacteria, and most nonphotosynthetic bacteria and protozoa, but is notably absent from animals, fungi, and yeasts. PEPC primarily plays an anaplerotic role by replenishing C4-dicarboxylic acids utilised for both energy and biosynthetic metabolisms.	Defined by 6 residues: HIS:A-138ARG:A-396GLU:A-506ASP:A-543ARG:A-581ARG:A-713 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.1.1.31 (PDB Primary Data) Search M-CSA Motif + EC 4.1.1.31

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.