4JLY

Dodecameric structure of spermidine N-acetyltransferase from Vibrio cholerae

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4jlya_	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	(Vibrio cholerae O1 biovar El Tor str. N16961 ) [TaxId: 243277 ],	SCOPe (2.08)
F	d4jlyf_	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	(Vibrio cholerae O1 biovar El Tor str. N16961 ) [TaxId: 243277 ],	SCOPe (2.08)
B	d4jlyb_	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	(Vibrio cholerae O1 biovar El Tor str. N16961 ) [TaxId: 243277 ],	SCOPe (2.08)
C	d4jlyc_	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	(Vibrio cholerae O1 biovar El Tor str. N16961 ) [TaxId: 243277 ],	SCOPe (2.08)
D	d4jlyd_	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	(Vibrio cholerae O1 biovar El Tor str. N16961 ) [TaxId: 243277 ],	SCOPe (2.08)
E	d4jlye_	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	(Vibrio cholerae O1 biovar El Tor str. N16961 ) [TaxId: 243277 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8060309	3000403	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8060309	3000403	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8060309	3000403	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8060309	3000403	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8060309	3000403	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8060309	3000403	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)
A	Acetyltransf_3_1	e4jlyA1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
F	Acetyltransf_3_1	e4jlyF1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
B	Acetyltransf_3_1	e4jlyB1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
C	Acetyltransf_3_1	e4jlyC1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
D	Acetyltransf_3_1	e4jlyD1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
E	Acetyltransf_3_1	e4jlyE1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
F	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
B	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
C	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
D	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
E	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	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	PF00583	Acetyltransferase (GNAT) family (Acetyltransf_1)	Acetyltransferase (GNAT) family	-	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	Spermidine n1-acetyltransferase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding acetyltransferase activity N-acetyltransferase activity acyltransferase activity diamine N-acetyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity N-acyltransferase activity	amine metabolic process catabolic process metabolic process cellular process polyamine catabolic process polyamine metabolic process biogenic amine catabolic process biogenic amine metabolic process amine catabolic process spermidine catabolic process spermidine metabolic process spermine catabolic process spermine metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR016181	Acyl-CoA N-acyltransferase	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR000182	GNAT domain	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.