1RA0

Bacterial cytosine deaminase D314G mutant bound to 5-fluoro-4-(S)-hydroxy-3,4-dihydropyrimidine.

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ra0a1	All beta proteins	Composite domain of metallo-dependent hydrolases	Composite domain of metallo-dependent hydrolases	Cytosine deaminase	Cytosine deaminase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1ra0a2	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	Cytosine deaminase catalytic domain	Cytosine deaminase catalytic domain	(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	SCOP2 Family	Cytosine deaminase	8029830	4003172	SCOP2 (2022-06-29)
A	SCOP2 Family	Cytosine deaminase catalytic domain	8029831	4003190	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Composite domain of metallo-dependent hydrolases	8042209	3000176	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Metallo-dependent hydrolases	8042210	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	PRK09230	e1ra0A1	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: PRK09230	ECOD (1.6)
A	Amidohydro_1_N	e1ra0A2	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF07969	Amidohydrolase family (Amidohydro_3)	Amidohydrolase family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Cytosine deaminase	isoguanine deaminase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines hydrolase activity catalytic activity deaminase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding isoguanine deaminase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines hydrolase activity catalytic activity deaminase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding zinc ion binding cytosine deaminase activity identical protein binding protein binding	pyrimidine-containing compound metabolic process catabolic process pyrimidine-containing compound catabolic process cytosine catabolic process primary metabolic process pyrimidine nucleobase catabolic process nucleobase-containing compound metabolic process pyrimidine nucleobase metabolic process nucleobase-containing small molecule metabolic process nucleobase catabolic process nucleobase metabolic process small molecule metabolic process metabolic process cellular process pyrimidine-containing compound metabolic process catabolic process pyrimidine-containing compound catabolic process cytosine catabolic process primary metabolic process pyrimidine nucleobase catabolic process nucleobase-containing compound metabolic process pyrimidine nucleobase metabolic process nucleobase-containing small molecule metabolic process nucleobase catabolic process nucleobase metabolic process small molecule metabolic process metabolic process cellular process cytosine metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR013108	Amidohydrolase 3	Domain
A	IPR011059	Metal-dependent hydrolase, composite domain superfamily	Homologous Superfamily
A	IPR052349	Metallo-dependent Hydrolases Superfamily Enzymes	Family
A	IPR032466	Metal-dependent hydrolase	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	cytosine deaminase (bacterial) M-CSA #710	Cytosine deaminase (CD) catalyses the deamination of cytosine to uracil and ammonia. It is an enzyme produced by bacteria and yeast, but not mammalian cells, and is a potential gene therapy agent. CD deaminates 5-fluorocytosine to potent antimetabolite 5-fluorouracil, which can block DNA replication in cells. Bacterial CD (bCD) is capable of deaminating a wide range of cytosine derivatives with varying efficiency. It is dependent of Fe2+ for maximal catalytic activity.	Defined by 6 residues: HIS:A-65 [auth A-61]HIS:A-67 [auth A-63]GLN:A-160 [auth A-156]HIS:A-218 [auth A-214]GLU:A-221 [auth A-217]ASP:A-317 [auth A-313] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.5.4.1 (PDB Primary Data) Search M-CSA Motif + EC 3.5.4.1 EC: 3.5.4 (UniProt) Search M-CSA Motif + EC 3.5.4

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.