3RG2

Structure of a two-domain NRPS fusion protein containing the EntE adenylation domain and EntB aryl-carrier protein from enterobactin biosynthesis

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00501	e3rg2A8	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
A	PF00550	e3rg2A10	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PF00550	ECOD (1.6)
A	PF13193	e3rg2A7	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
A	PF00501	e3rg2A9	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
B	PF00501	e3rg2B8	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
B	PF00550	e3rg2B10	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PF00550	ECOD (1.6)
B	PF13193	e3rg2B7	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
B	PF00501	e3rg2B9	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
C	PF00501	e3rg2C8	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
C	PF00550	e3rg2C10	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PF00550	ECOD (1.6)
C	PF13193	e3rg2C7	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
C	PF00501	e3rg2C9	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
D	PF00501	e3rg2D8	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
D	PF00550	e3rg2D10	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PF00550	ECOD (1.6)
D	PF13193	e3rg2D7	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
D	PF00501	e3rg2D9	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
E	PF00501	e3rg2E13	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
E	PF00550	e3rg2E15	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PF00550	ECOD (1.6)
E	PF13193	e3rg2E12	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
E	PF00501	e3rg2E14	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
F	PF00501	e3rg2F8	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
F	PF00550	e3rg2F10	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PF00550	ECOD (1.6)
F	PF13193	e3rg2F7	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
F	PF00501	e3rg2F9	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
G	PF00501	e3rg2G8	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
G	PF00550	e3rg2G10	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PF00550	ECOD (1.6)
G	PF13193	e3rg2G7	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
G	PF00501	e3rg2G9	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
H	PF00501	e3rg2H8	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
H	PF00550	e3rg2H10	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PF00550	ECOD (1.6)
H	PF13193	e3rg2H7	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
H	PF00501	e3rg2H9	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
I	PF00501	e3rg2I8	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
I	PF00550	e3rg2I10	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PF00550	ECOD (1.6)
I	PF13193	e3rg2I7	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
I	PF00501	e3rg2I9	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
J	PF00501	e3rg2J8	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)
J	PF00550	e3rg2J10	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PF00550	ECOD (1.6)
J	PF13193	e3rg2J7	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: PF13193	ECOD (1.6)
J	PF00501	e3rg2J9	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: PF00501	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
A	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
A	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	CATH (4.3.0)
B	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
B	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
B	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	CATH (4.3.0)
C	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
C	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
C	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	CATH (4.3.0)
D	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
D	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
D	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	CATH (4.3.0)
E	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
E	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
E	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	CATH (4.3.0)
F	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
F	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
F	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	CATH (4.3.0)
G	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
G	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
G	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	CATH (4.3.0)
H	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
H	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
H	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	CATH (4.3.0)
I	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
I	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
I	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	CATH (4.3.0)
J	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
J	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
J	1.10.1200.10	Mainly Alpha	Orthogonal Bundle	Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein	Chain A	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, G, H, I, J	PF00501	AMP-binding enzyme (AMP-binding)	AMP-binding enzyme	-	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	PF13193	AMP-binding enzyme C-terminal domain (AMP-binding_C)	AMP-binding enzyme C-terminal domain	This is a small domain that is found C terminal to Pfam:PF00501. It has a central beta sheet core that is flanked by alpha helices.	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	PF00550	Phosphopantetheine attachment site (PP-binding)	Phosphopantetheine attachment site	A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes memb ...	A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.	Domain

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, G, H, I, J	Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding 2,3-dihydroxybenzoate-serine ligase activity acid-amino acid ligase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity vitamin binding amide binding modified amino acid binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding 2,3-dihydroxybenzoate-serine ligase activity acid-amino acid ligase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity vitamin binding amide binding modified amino acid binding phosphopantetheine binding transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups identical protein binding protein binding isochorismatase activity leukotriene-A4 hydrolase activity ether hydrolase activity hydrolase activity, acting on ether bonds hydrolase activity adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding 2,3-dihydroxybenzoate--[aryl-carrier protein] ligase ligase activity, forming carbon-sulfur bonds acid-thiol ligase activity acyltransferase activity	enterobactin biosynthetic process polyketide metabolic process organic hydroxy compound metabolic process catechol-containing compound metabolic process secondary metabolic process antibiotic biosynthetic process siderophore biosynthetic process antibiotic metabolic process organic substance metabolic process secondary metabolite biosynthetic process siderophore metabolic process lactone biosynthetic process organic substance biosynthetic process catechol-containing compound biosynthetic process enterobactin biosynthetic process polyketide metabolic process organic hydroxy compound metabolic process catechol-containing compound metabolic process secondary metabolic process antibiotic biosynthetic process siderophore biosynthetic process antibiotic metabolic process organic substance metabolic process secondary metabolite biosynthetic process siderophore metabolic process lactone biosynthetic process organic substance biosynthetic process catechol-containing compound biosynthetic process catechol-containing siderophore biosynthetic process enterobactin metabolic process macrolide biosynthetic process macrolide metabolic process organic cyclic compound metabolic process biosynthetic process peptide biosynthetic process polyketide biosynthetic process lactone metabolic process organic hydroxy compound biosynthetic process phenol-containing compound metabolic process organic cyclic compound biosynthetic process phenol-containing compound biosynthetic process metabolic process nonribosomal peptide biosynthetic process peptide metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol cell periphery plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR009081	Phosphopantetheine binding ACP domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR000868	Isochorismatase-like	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR036380	Isochorismatase-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR036736	ACP-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR016291	Isochorismatase	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR011963	2,3-dihydroxybenzoate-AMP ligase	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR020845	AMP-binding, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR045851	AMP-binding enzyme, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR042099	ANL, N-terminal domain	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR025110	AMP-binding enzyme, C-terminal domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR000873	AMP-dependent synthetase/ligase domain	Domain