2BIF

6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE H256A MUTANT WITH F6P IN PHOSPHATASE ACTIVE SITE

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
B	d2bifb1	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, kinase domain	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, kinase domain	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
B	d2bifb2	Alpha and beta proteins (a/b)	Phosphoglycerate mutase-like	Phosphoglycerate mutase-like	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
A	d2bifa1	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, kinase domain	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, kinase domain	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
A	d2bifa2	Alpha and beta proteins (a/b)	Phosphoglycerate mutase-like	Phosphoglycerate mutase-like	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Histidine phosphatase-like	8019203	3000781	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	P-loop nucleotide/nucleoside kinase-like	8019199	3002021	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Histidine phosphatase-like	8019203	3000781	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	P-loop nucleotide/nucleoside kinase-like	8019199	3002021	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)
B	6PF2K	e2bifB1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: 6PF2K	ECOD (1.6)
B	His_Phos_1	e2bifB2	A: a/b three-layered sandwiches	X: Phosphoglycerate mutase-like (From Topology)	H: Phosphoglycerate mutase-like (From Topology)	T: Phosphoglycerate mutase-like	F: His_Phos_1	ECOD (1.6)
A	6PF2K	e2bifA1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: 6PF2K	ECOD (1.6)
A	His_Phos_1	e2bifA2	A: a/b three-layered sandwiches	X: Phosphoglycerate mutase-like (From Topology)	H: Phosphoglycerate mutase-like (From Topology)	T: Phosphoglycerate mutase-like	F: His_Phos_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
B	3.40.50.1240	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphoglycerate mutase-like	CATH (4.3.0)
A	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
A	3.40.50.1240	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphoglycerate mutase-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00300	Histidine phosphatase superfamily (branch 1) (His_Phos_1)	Histidine phosphatase superfamily (branch 1)	The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the p ...	The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PROTEIN (6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE)	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding carbohydrate kinase activity kinase activity phosphofructokinase activity transferase activity 6-phosphofructo-2-kinase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups phosphoric ester hydrolase activity fructose-2,6-bisphosphate 2-phosphatase activity hydrolase activity, acting on ester bonds carbohydrate phosphatase activity phosphatase activity hydrolase activity sugar-phosphatase activity	organophosphate metabolic process phosphate-containing compound metabolic process carbohydrate derivative metabolic process metabolic process cellular process phosphorus metabolic process fructose 2,6-bisphosphate metabolic process monosaccharide metabolic process carbohydrate metabolic process hexose metabolic process small molecule metabolic process primary metabolic process fructose metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR013078	Histidine phosphatase superfamily, clade-1	Family
A, B	IPR001345	Phosphoglycerate/bisphosphoglycerate mutase, active site	Active Site
A, B	IPR003094	Fructose-2,6-bisphosphatase	Family
A, B	IPR013079	6-phosphofructo-2-kinase	Domain
A, B	IPR029033	Histidine phosphatase superfamily	Homologous Superfamily
A, B	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	fructose-2,6-bisphosphate 2-phosphatase M-CSA #810	Fructose-6-phosphate-2-kinase/fructose-2,6-biphosphatase is a bifunctional enzyme. It is responsible to regulate the concentration of fructose-2,6-phosphate (Fru-2,6-P2), a potent physiological activator of phosphofructose kinase and an inhibitor of fructose-1,6-biphosphatase. Therefore, Fru-6-P,2-kinase/Fru-2,6-Pase is important in glucose homeostasis. The fructose-2,6-biphosphatase domain has been shown to be structurally and functionally homologous to phosphoglycerate mutase. It catalyses its reaction via a phosphoenzyme intermediate which utilises an active site histidine as a nucleophilic phosphoacceptor.	Defined by 6 residues: ARG:A-256 [auth A-255]ALA:A-257 [auth A-256]ASN:A-263 [auth A-262]ARG:A-306 [auth A-305]GLU:A-326 [auth A-325]HIS:A-391 [auth A-390] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.7.1.105 (PDB Primary Data) Search M-CSA Motif + EC 2.7.1.105 EC: 3.1.3.46 (PDB Primary Data) Search M-CSA Motif + EC 3.1.3.46

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.