1O98

1.4A CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE MUTASE FROM BACILLUS STEAROTHERMOPHILUS COMPLEXED WITH 2-PHOSPHOGLYCERATE

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)
A	d1o98a2	Alpha and beta proteins (a/b)	Alkaline phosphatase-like	Alkaline phosphatase-like	2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, catalytic domain	2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, catalytic domain	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
A	d1o98a1	Alpha and beta proteins (a/b)	2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain	2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain	2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain	2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	2 3-Bisphosphoglycerate-independent phosphoglycerate mutase	8021515	4003438	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Alkaline phosphatase-like	8033895	3001353	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	2 3-Bisphosphoglycerate-independent phosphoglycerate mutase substrate-binding domain	8033894	3000861	SCOP2 (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	PF01676	e1o98A1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: PF01676	ECOD (1.6)
A	PF06415	e1o98A2	A: a/b three-layered sandwiches	X: 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain (From Topology)	H: 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain (From Topology)	T: 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain	F: PF06415	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.1450.10	Alpha Beta	3-Layer(aba) Sandwich	2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain	BPG-independent phosphoglycerate mutase, domain B	CATH (4.3.0)
A	3.40.720.10	Alpha Beta	3-Layer(aba) Sandwich	Alkaline Phosphatase, subunit A	Alkaline Phosphatase, subunit A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01676	Metalloenzyme superfamily (Metalloenzyme)	Metalloenzyme superfamily	-	Family
A	PF06415	BPG-independent PGAM N-terminus (iPGM_N) (iPGM_N)	BPG-independent PGAM N-terminus (iPGM_N)	This family represents the N-terminal region of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (or phosphoglyceromutase or BPG-independent PGAM) protein (EC:5.4.2.1). The family is found in conjunction with Pfam:PF01676 (located in t ...	This family represents the N-terminal region of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (or phosphoglyceromutase or BPG-independent PGAM) protein (EC:5.4.2.1). The family is found in conjunction with Pfam:PF01676 (located in the C-terminal region of the protein).	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity isomerase activity phosphoglycerate mutase activity intramolecular phosphotransferase activity catalytic activity intramolecular transferase activity	ribonucleotide catabolic process pyridine nucleotide catabolic process oxoacid metabolic process carbohydrate catabolic process carbohydrate derivative metabolic process organophosphate catabolic process nucleoside phosphate catabolic process organic acid metabolic process nucleobase-containing compound metabolic process glycolytic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process purine ribonucleotide catabolic process ribonucleotide catabolic process pyridine nucleotide catabolic process oxoacid metabolic process carbohydrate catabolic process carbohydrate derivative metabolic process organophosphate catabolic process nucleoside phosphate catabolic process organic acid metabolic process nucleobase-containing compound metabolic process glycolytic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process purine ribonucleotide catabolic process phosphorus metabolic process pyridine nucleotide metabolic process nucleoside phosphate metabolic process organonitrogen compound catabolic process nicotinamide nucleotide metabolic process pyruvate metabolic process cellular metabolic process purine nucleoside diphosphate metabolic process primary metabolic process purine-containing compound catabolic process nucleotide metabolic process nucleobase-containing compound catabolic process organic cyclic compound metabolic process nucleoside diphosphate metabolic process purine nucleoside diphosphate catabolic process nucleoside diphosphate catabolic process metabolic process nucleoside triphosphate metabolic process monocarboxylic acid metabolic process purine ribonucleotide metabolic process pyridine-containing compound catabolic process ribose phosphate metabolic process catabolic process ATP metabolic process purine nucleotide metabolic process organic substance metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process purine ribonucleoside triphosphate metabolic process ribonucleoside diphosphate metabolic process ribonucleoside diphosphate catabolic process nucleotide catabolic process ribonucleoside triphosphate metabolic process purine nucleoside triphosphate metabolic process purine nucleotide catabolic process carbohydrate metabolic process carbohydrate derivative catabolic process organonitrogen compound metabolic process ADP catabolic process carboxylic acid metabolic process generation of precursor metabolites and energy organic cyclic compound catabolic process purine-containing compound metabolic process ADP metabolic process organophosphate metabolic process purine ribonucleoside diphosphate metabolic process cellular process organic substance catabolic process purine ribonucleoside diphosphate catabolic process monosaccharide metabolic process hexose catabolic process hexose metabolic process glucose catabolic process monosaccharide catabolic process small molecule catabolic process glucose metabolic process developmental process regulation of biological process regulation of developmental process biological regulation sporulation regulation of sporulation sporulation resulting in formation of a cellular spore anatomical structure morphogenesis anatomical structure formation involved in morphogenesis anatomical structure development	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011258	BPG-independent PGAM, N-terminal	Domain
A	IPR036646	BPG-independent phosphoglycerate mutase, domain B superfamily	Homologous Superfamily
A	IPR005995	Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent	Family
A	IPR006124	Metalloenzyme	Domain
A	IPR017850	Alkaline-phosphatase-like, core domain superfamily	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	phosphoglycerate mutase (2,3-bisphosphoglycerate-independent) M-CSA #738	Phosphoglycerate mutase catalyses a number of reactions, the most biologically relevant being the interconversion of glycerate-3-phosphate and glycerate-2-phosphate in the glycolysis and gluconeogenesis pathways.	Defined by 10 residues: ASP:A-12SER:A-62ASP:A-154ARG:A-261LYS:A-336ASP:A-403HIS:A-407ASP:A-444HIS:A-445HIS:A-462 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.4.2.1 (PDB Primary Data) Search M-CSA Motif + EC 5.4.2.1

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.