Function and Biology

Structure of Phycoerythrobilin Synthase PebS from the Cyanophage P-SSM2 in Complex with the bound Substrate Biliverdin IXa

Source organism: Prochlorococcus phage P-SSM2
Biochemical function: cobalt ion binding
Biological process: oxidation-reduction process
Cellular component: not assigned

EC 1.3.7.6: Phycoerythrobilin synthase

Reaction catalysed:
(3Z)-phycoerythrobilin + 2 oxidized ferredoxin = biliverdin IX-alpha + 2 reduced ferredoxin.
Comments:
  • This enzyme, from a cyanophage infecting oceanic cyanobacteria of the Prochlorococcus genus, uses a four-electron reduction to carry out the reactions catalyzed by EC 1.3.7.2 and EC 1.3.7.3.
  • 15,16-dihydrobiliverdin is formed as a bound intermediate.
  • Free 15,16-dihydrobiliverdin can also act as a substrate to form phycoerythrobilin.
Systematic name:
(3Z)-phycoerythrobilin:ferredoxin oxidoreductase (from biliverdin IX-alpha)
Alternative Name(s):
  • PebS

Sequence family

Pfam Protein family (Pfam)
PF05996
Domain description: Ferredoxin-dependent bilin reductase
Occurring in:
  1. Phycoerythrobilin synthase
1 copy of Pfam domain PF05996 (Ferredoxin-dependent bilin reductase) in Phycoerythrobilin synthase in PDB 2vck.

InterPro InterPro annotation
IPR009249
Domain description: Ferredoxin-dependent bilin reductase
Occurring in:
  1. Phycoerythrobilin synthase