Annotations: 4IST

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	GGACT_1	e4istA2	A: a+b two layers	X: BtrG-like (Pfam 03674) (From Topology)	H: BtrG-like (Pfam 03674) (From Topology)	T: BtrG-like (Pfam 03674)	F: GGACT_1	ECOD (1.6)
A	Amidase	e4istA1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
B	GGACT_1	e4istB2	A: a+b two layers	X: BtrG-like (Pfam 03674) (From Topology)	H: BtrG-like (Pfam 03674) (From Topology)	T: BtrG-like (Pfam 03674)	F: GGACT_1	ECOD (1.6)
B	Amidase	e4istB1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
A	1.20.58.1700	Mainly Alpha	Up-down Bundle	Methane Monooxygenase Hydroxylase	Chain G, domain 1	CATH (4.3.0)
A	3.10.490.10	Alpha Beta	Roll	Hypothetical upf0131 protein ytfp	Gamma-glutamyl cyclotransferase-like	CATH (4.3.0)
B	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
B	1.20.58.1700	Mainly Alpha	Up-down Bundle	Methane Monooxygenase Hydroxylase	Chain G, domain 1	CATH (4.3.0)
B	3.10.490.10	Alpha Beta	Roll	Hypothetical upf0131 protein ytfp	Gamma-glutamyl cyclotransferase-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01425	Amidase (Amidase)	Amidase	This entry represents the amidase signature domain that consists structurally of a core domain that is covered by alpha-helices. In most members, this is found as a standalone domain, while in others, such as Scytalone dehydratase-like protein Arp1, ...	This entry represents the amidase signature domain that consists structurally of a core domain that is covered by alpha-helices. In most members, this is found as a standalone domain, while in others, such as Scytalone dehydratase-like protein Arp1, it is found in association with other domains.	Domain
A, B	PF21986	Allophanate hydrolase C-terminal domain (AH_C)	Allophanate hydrolase C-terminal domain	Allophanate hydrolase (AH) converts allophanate to ammonium and carbon dioxide. The AH structure is composed of N- and C-terminal domains. These domains catalyze sequential reactions: the N-terminal domain converts allophanate to N-carboxycarbamate, ...	Allophanate hydrolase (AH) converts allophanate to ammonium and carbon dioxide. The AH structure is composed of N- and C-terminal domains. These domains catalyze sequential reactions: the N-terminal domain converts allophanate to N-carboxycarbamate, whereas the C-terminal domain converts it to carbon dioxide and ammonium [2]. The C-terminal domain folds into alpha/beta structure in which some of the beta-strands form a barrel-like shape.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Allophanate Hydrolase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides allophanate hydrolase activity hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds urea carboxylase activity ligase activity, forming carbon-nitrogen bonds ligase activity cation binding metal ion binding	small molecule metabolic process metabolic process cellular process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036928	Amidase signature (AS) superfamily	Homologous Superfamily
A, B	IPR005481	Biotin carboxylase-like, N-terminal domain	Domain
A, B	IPR014085	Allophanate hydrolase	Domain
A, B	IPR011761	ATP-grasp fold	Domain
A, B	IPR053844	Allophanate hydrolase, C-terminal domain	Domain
A, B	IPR003778	Carboxyltransferase domain, subdomain A and B	Domain
A, B	IPR029000	Cyclophilin-like domain superfamily	Homologous Superfamily
A, B	IPR011764	Biotin carboxylation domain	Domain
A, B	IPR023631	Amidase signature domain	Domain
A, B	IPR050856	Biotin-dependent Carboxylase Complex	Family
A, B	IPR005479	Carbamoyl phosphate synthase, ATP-binding domain	Domain
A, B	IPR014084	Urea carboxylase	Family
A, B	IPR005482	Biotin carboxylase, C-terminal	Domain
A, B	IPR003833	Carboxyltransferase domain, subdomain C and D	Domain
A, B	IPR016185	Pre-ATP-grasp domain superfamily	Homologous Superfamily
A, B	IPR011054	Rudiment single hybrid motif	Homologous Superfamily
A, B	IPR011053	Single hybrid motif	Homologous Superfamily
A, B	IPR001882	Biotin-binding site	Binding Site
A, B	IPR000089	Biotin/lipoyl attachment	Domain

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.