2XBL

Crystal structure of GmhA from Burkholderia pseudomallei in complex with product

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d2xblb_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	automated matches	automated matches	(Burkholderia pseudomallei K96243 ) [TaxId: 272560 ],	SCOPe (2.08)
A	d2xbla_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	automated matches	automated matches	(Burkholderia pseudomallei K96243 ) [TaxId: 272560 ],	SCOPe (2.08)
C	d2xblc_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	automated matches	automated matches	(Burkholderia pseudomallei K96243 ) [TaxId: 272560 ],	SCOPe (2.08)
D	d2xbld_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	automated matches	automated matches	(Burkholderia pseudomallei K96243 ) [TaxId: 272560 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8088718	3001397	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8088718	3001397	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8088718	3001397	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8088718	3001397	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	SIS	e2xblB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: SIS	ECOD (1.6)
A	SIS	e2xblA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: SIS	ECOD (1.6)
C	SIS	e2xblC1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: SIS	ECOD (1.6)
D	SIS	e2xblD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: SIS	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
A	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
C	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
D	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF13580	SIS domain (SIS_2)	SIS domain	SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	PHOSPHOHEPTOSE ISOMERASE	binding carbohydrate derivative binding cation binding transition metal ion binding zinc ion binding ion binding metal ion binding small molecule binding isomerase activity D-sedoheptulose 7-phosphate isomerase activity intramolecular phosphotransferase activity catalytic activity intramolecular transferase activity	carbohydrate derivative biosynthetic process carbohydrate derivative metabolic process D-glycero-D-manno-heptose 7-phosphate biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process D-glycero-D-manno-heptose 7-phosphate metabolic process carbohydrate metabolic process polysaccharide biosynthetic process carbohydrate biosynthetic process carbohydrate derivative biosynthetic process carbohydrate derivative metabolic process D-glycero-D-manno-heptose 7-phosphate biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process D-glycero-D-manno-heptose 7-phosphate metabolic process carbohydrate metabolic process polysaccharide biosynthetic process carbohydrate biosynthetic process primary metabolic process macromolecule biosynthetic process cellular component organization capsule organization polysaccharide metabolic process macromolecule metabolic process cellular component organization or biogenesis capsule polysaccharide biosynthetic process external encapsulating structure organization	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR046348	SIS domain superfamily	Homologous Superfamily
A, B, C, D	IPR004515	Phosphoheptose isomerase	Family
A, B, C, D	IPR050099	SIS family GmhA and DiaA subfamilies	Family
A, B, C, D	IPR001347	SIS domain	Domain
A, B, C, D	IPR035461	GmhA/DiaA	Family

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.