Annotations: 1J2U

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
D	d1j2ud_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
F	d1j2uf_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
A	d1j2ua_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
B	d1j2ub_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
C	d1j2uc_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
E	d1j2ue_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
D	SCOP2B Superfamily	Creatininase	8035599	3000410	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Creatininase	8035599	3000410	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Creatininase	8035599	3000410	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Creatininase	8035599	3000410	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Creatininase	8035599	3000410	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Creatininase	8035599	3000410	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)
D	Creatininase	e1j2uD1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)
F	Creatininase	e1j2uF1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)
A	Creatininase	e1j2uA1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)
B	Creatininase	e1j2uB1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)
C	Creatininase	e1j2uC1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)
E	Creatininase	e1j2uE1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
D	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)
F	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)
A	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)
B	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)
C	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)
E	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF02633	Creatinine amidohydrolase (Creatininase)	Creatinine amidohydrolase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	creatinine amidohydrolase	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding hydrolase activity creatininase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds zinc ion binding hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides	creatinine metabolic process catabolic process creatinine catabolic process lactam catabolic process metabolic process cellular process small molecule metabolic process amide metabolic process lactam metabolic process water-soluble vitamin biosynthetic process small molecule biosynthetic process flavin-containing compound metabolic process vitamin biosynthetic process riboflavin biosynthetic process creatinine metabolic process catabolic process creatinine catabolic process lactam catabolic process metabolic process cellular process small molecule metabolic process amide metabolic process lactam metabolic process water-soluble vitamin biosynthetic process small molecule biosynthetic process flavin-containing compound metabolic process vitamin biosynthetic process riboflavin biosynthetic process vitamin metabolic process flavin-containing compound biosynthetic process biosynthetic process water-soluble vitamin metabolic process riboflavin metabolic process monocarboxylic acid biosynthetic process creatine metabolic process oxoacid metabolic process creatine biosynthetic process modified amino acid biosynthetic process carboxylic acid metabolic process modified amino acid metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process monocarboxylic acid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR003785	Creatininase/formamide hydrolase	Family
A, B, C, D, E A, B, C, D, E, F	IPR024087	Creatininase-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR031034	Creatinine amidohydrolase	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	creatininase M-CSA #720	Creatininase (creatinine amidohydrolase) from Pseudomonas putida catalyses the conversion of creatinine to creatine. It is a member of the urease-related amidohydrolase superfamily. The enzyme enables the bacteria to use creatinine as a source of carbon and nitrogen. The biological molecule is trimer of dimers. The active site of each monomer contains a binuclear metal centre located at the bottom of a cleft. In the native form of the enzyme both metal sites are occupied by Zn²⁺ ions.	Defined by 7 residues: GLU:A-34HIS:A-36ASP:A-45HIS:A-120GLU:A-122HIS:A-178GLU:A-183 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.5.2.10 (PDB Primary Data) Search M-CSA Motif + EC 3.5.2.10

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.