6HF6

Crystal structure of the Protease 1 (E29A,E60A,E80A) from Pyrococcus horikoshii co-crystallized with Tb-Xo4.

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	d6hf6b_	Alpha and beta proteins (a/b)	Flavodoxin-like	Class I glutamine amidotransferase-like	DJ-1/PfpI	Intracellular protease	(Pyrococcus horikoshii OT3 ) [TaxId: 70601 ],	SCOPe (2.08)
A	d6hf6a_	Alpha and beta proteins (a/b)	Flavodoxin-like	Class I glutamine amidotransferase-like	DJ-1/PfpI	Intracellular protease	(Pyrococcus horikoshii OT3 ) [TaxId: 70601 ],	SCOPe (2.08)
C	d6hf6c_	Alpha and beta proteins (a/b)	Flavodoxin-like	Class I glutamine amidotransferase-like	DJ-1/PfpI	Intracellular protease	(Pyrococcus horikoshii OT3 ) [TaxId: 70601 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Class I glutamine amidotransferase-like	8044159	3001405	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Class I glutamine amidotransferase-like	8044159	3001405	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Class I glutamine amidotransferase-like	8044159	3001405	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	DJ-1_PfpI	e6hf6B1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: DJ-1_PfpI	ECOD (1.6)
A	DJ-1_PfpI	e6hf6A1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: DJ-1_PfpI	ECOD (1.6)
C	DJ-1_PfpI	e6hf6C1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: DJ-1_PfpI	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.880	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Class I glutamine amidotransferase (GATase) domain	CATH (utative)
A	3.40.50.880	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Class I glutamine amidotransferase (GATase) domain	CATH (utative)
C	3.40.50.880	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Class I glutamine amidotransferase (GATase) domain	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF01965	DJ-1/PfpI family (DJ-1_PfpI)	DJ-1/PfpI family	The family includes the protease PfpI Swiss:Q51732 [1]. This domain is also found in transcriptional regulators such as Swiss:Q9RJG8.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Deglycase PH1704	catalytic activity, acting on a protein protein deglycase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds peptidase activity	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR029062	Class I glutamine amidotransferase-like	Homologous Superfamily
A, B, C	IPR002818	DJ-1/PfpI	Domain
A, B, C	IPR053435	Peptidase C56 Deglycase	Family
A, B, C	IPR006286	Deglycase PfpI-like	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.