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Crystal structure of E. coli lipoate-protein ligase A in complex with octyl-amp and apoH-protein

Source organism: Escherichia coli K-12
Biochemical function: lipoyltransferase activity
Biological process: glycine decarboxylation via glycine cleavage system
Cellular component: cytosol

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EC 6.3.1.20: Lipoate--protein ligase

Reaction catalysed:
(1a) ATP + (R)-lipoate = lipoyl-AMP + diphosphate
Systematic name:
[Lipoyl-carrier protein]-L-lysine:lipoate ligase (AMP-forming)
Alternative Name(s):
  • LPL
  • LPL-B
  • Lipoate protein ligase
  • Lipoate-protein ligase A
  • LplA (gene name)
  • LplJ (gene name)

GO terms

Sequence families

Pfam Protein families (Pfam)
PF01597
Domain description: Glycine cleavage H-protein
Occurring in:
  1. Glycine cleavage system H protein
The deposited structure of PDB entry 3a7a contains 2 copies of Pfam domain PF01597 (Glycine cleavage H-protein) in Glycine cleavage system H protein. Showing 1 copy in chain B.

PF10437
Domain description: Bacterial lipoate protein ligase C-terminus
Occurring in:
  1. Lipoate-protein ligase A
The deposited structure of PDB entry 3a7a contains 2 copies of Pfam domain PF10437 (Bacterial lipoate protein ligase C-terminus) in Lipoate-protein ligase A. Showing 1 copy in chain A.

PF21948
Domain description: Lipoyl protein ligase A/B catalytic domain
Occurring in:
  1. Lipoate-protein ligase A

InterPro InterPro annotations
IPR033753
Domain description: Glycine cleavage system H-protein/Simiate
Occurring in:
  1. Glycine cleavage system H protein
IPR002930
Domain description: Glycine cleavage system H-protein
Occurring in:
  1. Glycine cleavage system H protein
IPR004143
Domain description: Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
Occurring in:
  1. Lipoate-protein ligase A
IPR004562
Domain description: Lipoyltransferase/lipoate-protein ligase
Occurring in:
  1. Lipoate-protein ligase A
IPR045864
Domain description: Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
Occurring in:
  1. Lipoate-protein ligase A
IPR003016
Domain description: 2-oxo acid dehydrogenase, lipoyl-binding site
Occurring in:
  1. Glycine cleavage system H protein
IPR000089
Domain description: Biotin/lipoyl attachment
Occurring in:
  1. Glycine cleavage system H protein
IPR011053
Domain description: Single hybrid motif
Occurring in:
  1. Glycine cleavage system H protein
IPR017453
Domain description: Glycine cleavage system H-protein, subgroup
Occurring in:
  1. Glycine cleavage system H protein
IPR019491
Domain description: Lipoate protein ligase, C-terminal
Occurring in:
  1. Lipoate-protein ligase A
IPR023741
Domain description: Lipoate-protein ligase A
Occurring in:
  1. Lipoate-protein ligase A

Structure domains

CATH CATH domains
2.40.50.100
Class: Mainly Beta
Architecture: Beta Barrel
Topology: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homology: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Occurring in:
  1. Glycine cleavage system H protein
The deposited structure of PDB entry 3a7a contains 2 copies of CATH domain 2.40.50.100 (OB fold (Dihydrolipoamide Acetyltransferase, E2P)) in Glycine cleavage system H protein. Showing 1 copy in chain B.
3.30.390.50
Class: Alpha Beta
Architecture: 2-Layer Sandwich
Topology: Enolase-like; domain 1
Homology: CO dehydrogenase flavoprotein, C-terminal domain
Occurring in:
  1. Lipoate-protein ligase A
The deposited structure of PDB entry 3a7a contains 2 copies of CATH domain 3.30.390.50 (Enolase-like; domain 1) in Lipoate-protein ligase A. Showing 1 copy in chain A.
3.30.930.10
Class: Alpha Beta
Architecture: 2-Layer Sandwich
Topology: BirA Bifunctional Protein; domain 2
Homology: Bira Bifunctional Protein; Domain 2
Occurring in:
  1. Lipoate-protein ligase A
The deposited structure of PDB entry 3a7a contains 2 copies of CATH domain 3.30.930.10 (BirA Bifunctional Protein; domain 2) in Lipoate-protein ligase A. Showing 1 copy in chain A.

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