4UBP

STRUCTURE OF BACILLUS PASTEURII UREASE INHIBITED WITH ACETOHYDROXAMIC ACID AT 1.55 A RESOLUTION

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
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4ubpa_	Alpha and beta proteins (a+b)	Urease, gamma-subunit	Urease, gamma-subunit	Urease, gamma-subunit	Urease, gamma-subunit	(Sporosarcina pasteurii ) [TaxId: 1474 ],	SCOPe (2.08)
B	d4ubpb_	All beta proteins	beta-clip	Urease, beta-subunit	Urease, beta-subunit	Urease, beta-subunit	(Sporosarcina pasteurii ) [TaxId: 1474 ],	SCOPe (2.08)
C	d4ubpc1	All beta proteins	Composite domain of metallo-dependent hydrolases	Composite domain of metallo-dependent hydrolases	alpha-Subunit of urease	alpha-Subunit of urease	(Sporosarcina pasteurii ) [TaxId: 1474 ],	SCOPe (2.08)
C	d4ubpc2	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	alpha-subunit of urease, catalytic domain	alpha-subunit of urease, catalytic domain	(Sporosarcina pasteurii ) [TaxId: 1474 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Urease, gamma-subunit	8021867	4000909	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Urease, gamma-subunit	8034247	3001945	SCOP2 (2022-06-29)
B	SCOP2 Family	Urease, beta-subunit	8030752	4002967	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Urease, beta-subunit	8043131	3001949	SCOP2 (2022-06-29)
C	SCOP2 Family	alpha-Subunit of urease	8030793	4003022	SCOP2 (2022-06-29)
C	SCOP2 Family	alpha-subunit of urease, catalytic domain	8031052	4003208	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Composite domain of metallo-dependent hydrolases	8043172	3000176	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Metallo-dependent hydrolases	8043430	3000428	SCOP2 (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	Urease_gamma	e4ubpA1	A: a+b two layers	X: Urease, gamma-subunit (From Topology)	H: Urease, gamma-subunit (From Topology)	T: Urease, gamma-subunit	F: Urease_gamma	ECOD (1.6)
B	Urease_beta	e4ubpB1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Urease, beta-subunit (From Topology)	T: Urease, beta-subunit	F: Urease_beta	ECOD (1.6)
C	Urease_alpha	e4ubpC1	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: Urease_alpha	ECOD (1.6)
C	Amidohydro_1_N	e4ubpC2	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	3.30.280.10	Alpha Beta	2-Layer Sandwich	Urease	subunit A	CATH (4.3.0)
B	2.10.150.10	Mainly Beta	Ribbon	Urease, subunit B	Urease, beta subunit	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00547	Urease, gamma subunit (Urease_gamma)	Urease, gamma subunit	Urease is a nickel-binding enzyme that catalyses the hydrolysis of urea to carbon dioxide and ammonia.	Domain
B	PF00699	Urease beta subunit (Urease_beta)	Urease beta subunit	This subunit is known as alpha in Heliobacter.	Domain
C	PF00449	Urease alpha-subunit, N-terminal domain (Urease_alpha)	Urease alpha-subunit, N-terminal domain	The N-terminal domain is a composite domain and plays a major trimer stabilising role by contacting the catalytic domain of the symmetry related alpha-subunit.	Domain
C	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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PROTEIN (UREASE (CHAIN A))	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity urease activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds cation binding transition metal ion binding ion binding binding nickel cation binding metal ion binding small molecule binding	nitrogen cycle metabolic process catabolic process amide catabolic process small molecule metabolic process metabolic process urea catabolic process amide metabolic process small molecule catabolic process urea metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity
B	PROTEIN (UREASE (CHAIN B))	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity urease activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds	nitrogen cycle metabolic process catabolic process amide catabolic process small molecule metabolic process metabolic process urea catabolic process amide metabolic process small molecule catabolic process urea metabolic process	protein-containing complex intracellular anatomical structure catalytic complex cytoplasm cellular anatomical entity urease complex
C	PROTEIN (UREASE (CHAIN C))	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity urease activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds cation binding transition metal ion binding ion binding binding nickel cation binding metal ion binding small molecule binding	nitrogen cycle metabolic process catabolic process amide catabolic process small molecule metabolic process metabolic process urea catabolic process amide metabolic process small molecule catabolic process urea metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR050069	Urease subunit	Family
A	IPR012010	Urease, gamma subunit	Family
A	IPR002026	Urease, gamma/gamma-beta subunit	Family
A	IPR036463	Urease, gamma subunit superfamily	Homologous Superfamily
B	IPR002019	Urease, beta subunit-like	Family
B	IPR050069	Urease subunit	Family
B	IPR036461	Urease, beta subunit superfamily	Homologous Superfamily
C	IPR029754	Urease nickel binding site	Binding Site
C	IPR017950	Urease active site	Active Site
C	IPR006680	Amidohydrolase-related	Domain
C	IPR011059	Metal-dependent hydrolase, composite domain superfamily	Homologous Superfamily
C	IPR032466	Metal-dependent hydrolase	Homologous Superfamily
C	IPR011612	Urease alpha-subunit, N-terminal domain	Domain
C	IPR050112	Urease Alpha Subunit	Family
C	IPR005848	Urease, alpha subunit	Family
C	IPR017951	Urease alpha subunit, C-terminal	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	ACE	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 PSI-MOD : N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359
C	KCX	Parent Component: LYS RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354

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.