Annotations: 5G4A

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	DUF4111	e5g4aB2	A: alpha arrays	X: Aminoglycoside adenyltransferase AadA C-terminal domain (From Topology)	H: Aminoglycoside adenyltransferase AadA C-terminal domain (From Topology)	T: Aminoglycoside adenyltransferase AadA C-terminal domain	F: DUF4111	ECOD (1.6)
B	NTP_transf_2	e5g4aB1	A: a+b three layers	X: Nucleotidyltransferase-like	H: Nucleotidyltransferase (From Topology)	T: Nucleotidyltransferase	F: NTP_transf_2	ECOD (1.6)
A	DUF4111	e5g4aA2	A: alpha arrays	X: Aminoglycoside adenyltransferase AadA C-terminal domain (From Topology)	H: Aminoglycoside adenyltransferase AadA C-terminal domain (From Topology)	T: Aminoglycoside adenyltransferase AadA C-terminal domain	F: DUF4111	ECOD (1.6)
A	NTP_transf_2	e5g4aA1	A: a+b three layers	X: Nucleotidyltransferase-like	H: Nucleotidyltransferase (From Topology)	T: Nucleotidyltransferase	F: NTP_transf_2	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B	PF13427	Aminoglycoside adenylyltransferase, C-terminal domain (AadA_C)	Aminoglycoside adenylyltransferase, C-terminal domain	This domain is found at the C-terminal end of Aminoglycoside adenylyltransferase from Salmonella typhimurium (AadA) and other proteins associated with methicillin-resistant bacteria. AadA adenylates the 3''-hydroxyl group of the streptomycin glucosam ...	This domain is found at the C-terminal end of Aminoglycoside adenylyltransferase from Salmonella typhimurium (AadA) and other proteins associated with methicillin-resistant bacteria. AadA adenylates the 3''-hydroxyl group of the streptomycin glucosamine ring and the 9-hydroxyl group of the spectinomycin actinamine ring, mediating bacterial resistance to these antibiotics. This enzyme is organised into two domains: a N-terminal domain with a nucleotidyltransferase fold (Pfam:PF01909) and a C-terminal domain (this entry) which consists of five alpha-helices forming an up-and-down alpha-helical bundle. This domain undergoes small conformational changes upon binding of ATP and magnesium that play a key role in the binding of the antibiotic compounds [1,2].	Domain
B	PF01909	Nucleotidyltransferase domain (NTP_transf_2)	Nucleotidyltransferase domain	Members of this family belong to a large family of nucleotidyltransferases [1]. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTa ...	Members of this family belong to a large family of nucleotidyltransferases [1]. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.	Domain
A	PF13427	Aminoglycoside adenylyltransferase, C-terminal domain (AadA_C)	Aminoglycoside adenylyltransferase, C-terminal domain	This domain is found at the C-terminal end of Aminoglycoside adenylyltransferase from Salmonella typhimurium (AadA) and other proteins associated with methicillin-resistant bacteria. AadA adenylates the 3''-hydroxyl group of the streptomycin glucosam ...	This domain is found at the C-terminal end of Aminoglycoside adenylyltransferase from Salmonella typhimurium (AadA) and other proteins associated with methicillin-resistant bacteria. AadA adenylates the 3''-hydroxyl group of the streptomycin glucosamine ring and the 9-hydroxyl group of the spectinomycin actinamine ring, mediating bacterial resistance to these antibiotics. This enzyme is organised into two domains: a N-terminal domain with a nucleotidyltransferase fold (Pfam:PF01909) and a C-terminal domain (this entry) which consists of five alpha-helices forming an up-and-down alpha-helical bundle. This domain undergoes small conformational changes upon binding of ATP and magnesium that play a key role in the binding of the antibiotic compounds [1,2].	Domain
A	PF01909	Nucleotidyltransferase domain (NTP_transf_2)	Nucleotidyltransferase domain	Members of this family belong to a large family of nucleotidyltransferases [1]. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTa ...	Members of this family belong to a large family of nucleotidyltransferases [1]. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B	Aminoglycoside (3'') (9) adenylyltransferase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding adenylyltransferase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups cation binding metal ion binding aminoglycoside 3''-adenylyltransferase activity aminoglycoside nucleotidyltransferase activity	response to stimulus response to chemical response to antibiotic	-
A	Aminoglycoside (3'') (9) adenylyltransferase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding adenylyltransferase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups cation binding metal ion binding aminoglycoside 3''-adenylyltransferase activity aminoglycoside nucleotidyltransferase activity	response to stimulus response to chemical response to antibiotic	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B	IPR043519	Nucleotidyltransferase superfamily	Homologous Superfamily
B	IPR002934	Polymerase, nucleotidyl transferase domain	Domain
B	IPR024172	Adenylyltransferase AadA/Aad9	Family
B	IPR025184	Adenylyltransferase AadA, C-terminal domain	Domain
A	IPR043519	Nucleotidyltransferase superfamily	Homologous Superfamily
A	IPR002934	Polymerase, nucleotidyl transferase domain	Domain
A	IPR024172	Adenylyltransferase AadA/Aad9	Family
A	IPR025184	Adenylyltransferase AadA, C-terminal domain	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
B	CME	Parent Component: CYS
B	CSS	Parent Component: CYS RESID: AA0269 PSI-MOD : L-cysteine persulfide MOD:00274
A	CME	Parent Component: CYS RESID: AA0269
A	CSS	Parent Component: CYS RESID: AA0269 , AA0269 PSI-MOD : L-cysteine persulfide MOD:00274 , L-cysteine persulfide MOD:00274

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.