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Crystal structure of lipoate-protein ligase A bound with lipoyl-AMP

Source organism: Thermoplasma acidophilum
Biochemical function: not assigned
Biological process: not assigned
Cellular component: not assigned

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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

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF21948
Domain description: Lipoyl protein ligase A/B catalytic domain
Occurring in:
  1. Lipoate-protein ligase A subunit 1

InterPro InterPro annotations
IPR004143
Domain description: Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
Occurring in:
  1. Lipoate-protein ligase A subunit 1
IPR045864
Domain description: Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
Occurring in:
  1. Lipoate-protein ligase A subunit 1

Structure domain

CATH CATH domain
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 subunit 1
The deposited structure of PDB entry 2art contains 1 copy of CATH domain 3.30.930.10 (BirA Bifunctional Protein; domain 2) in Lipoate-protein ligase A subunit 1. Showing 1 copy in chain A.
SCOP SCOP annotation
143642
Class: Alpha and beta proteins (a+b)
Fold: Class II aaRS and biotin synthetases
Superfamily: Class II aaRS and biotin synthetases
Occurring in:
  1. Lipoate-protein ligase A subunit 1
The deposited structure of PDB entry 2art contains 1 copy of SCOP domain 143642 (LplA-like) in Lipoate-protein ligase A subunit 1. Showing 1 copy in chain A.

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