4RDV | pdb_00004rdv

The structure of N-formimino-L-Glutamate Iminohydrolase from Pseudomonas aeruginosa complexed with N-formimino-L-Aspartate

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Amidohydro_1_C_2,PRK09229	e4rdvA2	A: beta sandwiches	X: Composite domain of metallo-dependent hydrolases (From Topology)	H: Composite domain of metallo-dependent hydrolases (From Topology)	T: Composite domain of metallo-dependent hydrolases	F: Amidohydro_1_C_2,PRK09229	ECOD (1.6)
A	Amidohydro_1_N	e4rdvA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Amidohydro_1_N	ECOD (1.6)
B	Amidohydro_1_C_2,PRK09229	e4rdvB1	A: beta sandwiches	X: Composite domain of metallo-dependent hydrolases (From Topology)	H: Composite domain of metallo-dependent hydrolases (From Topology)	T: Composite domain of metallo-dependent hydrolases	F: Amidohydro_1_C_2,PRK09229	ECOD (1.6)
B	Amidohydro_1_N	e4rdvB2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Amidohydro_1_N	ECOD (1.6)
C	Amidohydro_1_C_2,PRK09229	e4rdvC1	A: beta sandwiches	X: Composite domain of metallo-dependent hydrolases (From Topology)	H: Composite domain of metallo-dependent hydrolases (From Topology)	T: Composite domain of metallo-dependent hydrolases	F: Amidohydro_1_C_2,PRK09229	ECOD (1.6)
C	Amidohydro_1_N	e4rdvC2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Amidohydro_1_N	ECOD (1.6)
D	Amidohydro_1_C_2,PRK09229	e4rdvD1	A: beta sandwiches	X: Composite domain of metallo-dependent hydrolases (From Topology)	H: Composite domain of metallo-dependent hydrolases (From Topology)	T: Composite domain of metallo-dependent hydrolases	F: Amidohydro_1_C_2,PRK09229	ECOD (1.6)
D	Amidohydro_1_N	e4rdvD2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Amidohydro_1_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.30.40.10	Mainly Beta	Roll	Urease, subunit C	domain 1	CATH (4.3.0)
A	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)
B	2.30.40.10	Mainly Beta	Roll	Urease, subunit C	domain 1	CATH (4.3.0)
B	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)
C	2.30.40.10	Mainly Beta	Roll	Urease, subunit C	domain 1	CATH (4.3.0)
C	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)
D	2.30.40.10	Mainly Beta	Roll	Urease, subunit C	domain 1	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	PF01979	Amidohydrolase family (Amidohydro_1)	Amidohydrolase family	This family of enzymes are a a large metal dependent hydrolase superfamily [1]. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisatio ...	This family of enzymes are a a large metal dependent hydrolase superfamily [1]. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisation as a purine and also as a nitrogen source [2]. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyse the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit [3]. Dihydroorotases (EC:3.5.2.3) are also included [4-5].	Domain
A, B, C, D	PF22429	Formimidoylglutamate deiminase HutF, N-terminal domain (HutF_N)	Formimidoylglutamate deiminase HutF, N-terminal domain	This small domain is found at the N-terminal end of Formimidoylglutamate deiminase from Pseudomonas aeruginosa (also known as N-formimino-L-Glutamate Iminohydrolase, HutF) and similar proteins predominantly found in proteobacteria. HutF catalyzes he ...	This small domain is found at the N-terminal end of Formimidoylglutamate deiminase from Pseudomonas aeruginosa (also known as N-formimino-L-Glutamate Iminohydrolase, HutF) and similar proteins predominantly found in proteobacteria. HutF catalyzes he deamination of N-formimino-l-glutamate to N-formyl-l-glutamate and ammonia in the histidine degradation pathway [1]. The domain represented by this entry folds into an open beta-barrel which is completed by two strands located at the C terminus of the protein.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	N-FORMIMINO-L-GLUTAMATE IMINOHYDROLASE	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines formimidoylglutamate deiminase activity hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds deaminase activity cation binding ion binding binding metal ion binding small molecule binding	catabolic process oxoacid metabolic process aromatic amino acid family catabolic process amino acid metabolic process organic acid catabolic process organic acid metabolic process imidazole-containing compound metabolic process alpha-amino acid metabolic process carboxylic acid catabolic process small molecule metabolic process amino acid catabolic process aromatic amino acid metabolic process L-histidine metabolic process imidazole-containing compound catabolic process catabolic process oxoacid metabolic process aromatic amino acid family catabolic process amino acid metabolic process organic acid catabolic process organic acid metabolic process imidazole-containing compound metabolic process alpha-amino acid metabolic process carboxylic acid catabolic process small molecule metabolic process amino acid catabolic process aromatic amino acid metabolic process L-histidine metabolic process imidazole-containing compound catabolic process L-amino acid catabolic process carboxylic acid metabolic process primary metabolic process L-amino acid metabolic process L-histidine catabolic process proteinogenic amino acid metabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process metabolic process cellular process small molecule catabolic process glutamine family amino acid metabolic process glutamate metabolic process L-histidine catabolic process to glutamate and formate dicarboxylic acid metabolic process monocarboxylic acid metabolic process formate metabolic process L-histidine catabolic process to glutamate and formamide amide catabolic process amide metabolic process formamide metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR055156	Formimidoylglutamate deiminase, N-terminal domain	Domain
A, B, C, D	IPR006680	Amidohydrolase-related	Domain
A, B, C, D	IPR011059	Metal-dependent hydrolase, composite domain superfamily	Homologous Superfamily
A, B, C, D	IPR032466	Metal-dependent hydrolase	Homologous Superfamily
A, B, C, D	IPR051607	Metallo-dependent Hydrolases	Family
A, B, C, D	IPR010252	Formimidoylglutamate deiminase	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.