3IJ6

CRYSTAL STRUCTURE OF AN UNCHARACTERIZED METAL-DEPENDENT HYDROLASE FROM Lactobacillus acidophilus

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d3ij6a1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	automated matches	automated matches	(Lactobacillus acidophilus ) [TaxId: 1579 ],	SCOPe (2.08)
A	d3ij6a2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Lactobacillus acidophilus ) [TaxId: 1579 ],	SCOPe (2.08)
B	d3ij6b1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	automated matches	automated matches	(Lactobacillus acidophilus ) [TaxId: 1579 ],	SCOPe (2.08)
B	d3ij6b2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Lactobacillus acidophilus ) [TaxId: 1579 ],	SCOPe (2.08)
C	d3ij6c1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	automated matches	automated matches	(Lactobacillus acidophilus ) [TaxId: 1579 ],	SCOPe (2.08)
C	d3ij6c2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Lactobacillus acidophilus ) [TaxId: 1579 ],	SCOPe (2.08)
D	d3ij6d1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	automated matches	automated matches	(Lactobacillus acidophilus ) [TaxId: 1579 ],	SCOPe (2.08)
D	d3ij6d2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Lactobacillus acidophilus ) [TaxId: 1579 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF04909	e3ij6A1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF04909	ECOD (1.6)
B	PF04909	e3ij6B1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF04909	ECOD (1.6)
C	PF04909	e3ij6C1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF04909	ECOD (1.6)
D	PF04909	e3ij6D1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF04909	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)
B	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)
C	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)
D	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF04909	Amidohydrolase (Amidohydro_2)	Amidohydrolase	These proteins are amidohydrolases that are related to Pfam:PF01979 [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	UNCHARACTERIZED METAL-DEPENDENT HYDROLASE	hydrolase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding carboxy-lyase activity lyase activity carbon-carbon lyase activity	organic substance metabolic process metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR032465	2-amino-3-carboxymuconate-6-semialdehyde decarboxylase	Family
A, B, C, D	IPR006680	Amidohydrolase-related	Domain
A, B, C, D	IPR032466	Metal-dependent hydrolase	Homologous Superfamily

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.