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Crystal structure of Escherichia coli Flavin trafficking protein, an FMN transferase, Y60N mutant, ADP-inhibited

Source organism: Escherichia coli K-12
Biochemical function: metal ion binding
Biological process: protein flavinylation
Cellular component: oxidoreductase complex

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EC 2.7.1.180: FAD:protein FMN transferase

Reaction catalysed:
FAD + [protein]-L-threonine = [protein]-FMN-L-threonine + AMP
Systematic name:
FAD:protein riboflavin-5'-phosphate transferase
Alternative Name(s):
  • ApbE (gene name)
  • Flavin transferase

GO terms

Sequence family

Pfam Protein family (Pfam)
PF02424
Domain description: ApbE family
Occurring in:
  1. FAD:protein FMN transferase
The deposited structure of PDB entry 4xgx contains 2 copies of Pfam domain PF02424 (ApbE family) in FAD:protein FMN transferase. Showing 1 copy in chain B.

InterPro InterPro annotations
IPR024932
Domain description: Flavin transferase ApbE
Occurring in:
  1. FAD:protein FMN transferase
IPR003374
Domain description: ApbE-like superfamily
Occurring in:
  1. FAD:protein FMN transferase

Structure domain

CATH CATH domain
3.10.520.10
Class: Alpha Beta
Architecture: Roll
Topology: T-fold
Homology: ApbE-like domains
Occurring in:
  1. FAD:protein FMN transferase
The deposited structure of PDB entry 4xgx contains 2 copies of CATH domain 3.10.520.10 (T-fold) in FAD:protein FMN transferase. Showing 1 copy in chain B.

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