5ICL

Crystal structure of Enterococcus faecalis lipoate-protein ligase A (lplA-2) in complex with lipoyl-AMP

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
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	d5icla1	Alpha and beta proteins (a+b)	Class II aaRS and biotin synthetases	Class II aaRS and biotin synthetases	automated matches	automated matches	(Enterococcus faecalis V583 ) [TaxId: 226185 ],	SCOPe (2.08)
A	d5icla2	Alpha and beta proteins (a+b)	SufE/NifU	SufE/NifU	automated matches	automated matches	(Enterococcus faecalis V583 ) [TaxId: 226185 ],	SCOPe (2.08)
A	d5icla3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Enterococcus faecalis V583 ) [TaxId: 226185 ],	SCOPe (2.08)
B	d5iclb1	Alpha and beta proteins (a+b)	Class II aaRS and biotin synthetases	Class II aaRS and biotin synthetases	automated matches	automated matches	(Enterococcus faecalis V583 ) [TaxId: 226185 ],	SCOPe (2.08)
B	d5iclb2	Alpha and beta proteins (a+b)	SufE/NifU	SufE/NifU	automated matches	automated matches	(Enterococcus faecalis V583 ) [TaxId: 226185 ],	SCOPe (2.08)
B	d5iclb3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Enterococcus faecalis V583 ) [TaxId: 226185 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Lip_prot_lig_C	e5iclA2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: SufE/NifU (From Topology)	T: SufE/NifU	F: Lip_prot_lig_C	ECOD (1.6)
A	BPL_LplA_LipB_1	e5iclA1	A: a+b three layers	X: Class II aaRS and biotin synthetases (From Topology)	H: Class II aaRS and biotin synthetases (From Topology)	T: Class II aaRS and biotin synthetases	F: BPL_LplA_LipB_1	ECOD (1.6)
B	Lip_prot_lig_C	e5iclB2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: SufE/NifU (From Topology)	T: SufE/NifU	F: Lip_prot_lig_C	ECOD (1.6)
B	BPL_LplA_LipB_1	e5iclB1	A: a+b three layers	X: Class II aaRS and biotin synthetases (From Topology)	H: Class II aaRS and biotin synthetases (From Topology)	T: Class II aaRS and biotin synthetases	F: BPL_LplA_LipB_1	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF21948	Lipoyl protein ligase A/B catalytic domain (LplA-B_cat)	Lipoyl protein ligase A/B catalytic domain	This entry represents the catalytic domain of a group of lipoyl ligases/lipoyltransferases, such as Lipoate-protein ligase A/B (LipA/B) from E.coli and mammalian lipoyltransferases [1-5]. These proteins catalyse the transfer of the lipoyl group from ...	This entry represents the catalytic domain of a group of lipoyl ligases/lipoyltransferases, such as Lipoate-protein ligase A/B (LipA/B) from E.coli and mammalian lipoyltransferases [1-5]. These proteins catalyse the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of lipoate-dependent enzymes. Lipoic acid is an essential cofactor of the alpha-ketoacid dehydrogenase complexes and the glycine cleavage system.	Domain
A, B	PF10437	Bacterial lipoate protein ligase C-terminus (Lip_prot_lig_C)	Bacterial lipoate protein ligase C-terminus	This is the C-terminal domain of a bacterial lipoate protein ligase. There is no conservation between this C-terminus and that of vertebrate lipoate protein ligase C-termini, but both are associated with the domain BPL_LipA_LipB Pfam:PF03099, furthe ...	This is the C-terminal domain of a bacterial lipoate protein ligase. There is no conservation between this C-terminus and that of vertebrate lipoate protein ligase C-termini, but both are associated with the domain BPL_LipA_LipB Pfam:PF03099, further upstream. This domain is required for adenylation of lipoic acid by lipoate protein ligases. The domain is not required for transfer of lipoic acid from the adenylate to the lipoyl domain. Upon adenylation, this domain rotates 180 degrees away from the active site cleft. Therefore, the domain does not interact with the lipoyl domain during transfer.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Lipoate--protein ligase	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 lipoyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity catalytic activity, acting on a protein lipoate-protein ligase activity nucleotidyltransferase activity ligase activity, forming carbon-nitrogen bonds transferase activity, transferring phosphorus-containing groups ligase activity	-	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR004143	Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain	Domain
A, B	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)	Homologous Superfamily
A, B	IPR019491	Lipoate protein ligase, C-terminal	Domain
A, B	IPR004562	Lipoyltransferase/lipoate-protein ligase	Family

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.