5TIC

X-ray structure of wild-type E. coli Acyl-CoA thioesterase I at pH 5

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)
A	d5tica1	Alpha and beta proteins (a/b)	Flavodoxin-like	SGNH hydrolase	TAP-like	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d5tica2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d5ticb1	Alpha and beta proteins (a/b)	Flavodoxin-like	SGNH hydrolase	TAP-like	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d5ticb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(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	SGNH hydrolase-like	8097992	3001315	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	SGNH hydrolase-like	8097992	3001315	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	Lipase_GDSL_2	e5ticA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: SGNH hydrolase (From Topology)	T: SGNH hydrolase	F: Lipase_GDSL_2	ECOD (1.6)
B	Lipase_GDSL_2	e5ticB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: SGNH hydrolase (From Topology)	T: SGNH hydrolase	F: Lipase_GDSL_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1110	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	SGNH hydrolase	CATH (4.3.0)
B	3.40.50.1110	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	SGNH hydrolase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00657	GDSL-like Lipase/Acylhydrolase (Lipase_GDSL)	GDSL-like Lipase/Acylhydrolase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Acyl-CoA thioesterase I	fatty acyl-[ACP] hydrolase activity hydrolase activity, acting on ester bonds thiolester hydrolase activity hydrolase activity catalytic activity peptidase activity catalytic activity, acting on a protein fatty acyl-CoA hydrolase activity long-chain fatty acyl-CoA hydrolase activity acyl-CoA hydrolase activity arylesterase activity carboxylic ester hydrolase activity identical protein binding protein binding fatty acyl-[ACP] hydrolase activity hydrolase activity, acting on ester bonds thiolester hydrolase activity hydrolase activity catalytic activity peptidase activity catalytic activity, acting on a protein fatty acyl-CoA hydrolase activity long-chain fatty acyl-CoA hydrolase activity acyl-CoA hydrolase activity arylesterase activity carboxylic ester hydrolase activity identical protein binding protein binding binding lysophospholipase activity phospholipase activity lipase activity	primary metabolic process metabolic process lipid metabolic process proteolysis protein metabolic process macromolecule metabolic process	outer membrane-bounded periplasmic space cell envelope periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036514	SGNH hydrolase superfamily	Homologous Superfamily
A, B	IPR051532	Diverse Ester Hydrolysis Enzymes	Family
A, B	IPR008265	Lipase, GDSL, active site	Active Site
A, B	IPR013830	SGNH hydrolase-type esterase domain	Domain

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.