D
IPR013580

Light-independent protochlorophyllide reductase subunit B-like, C-terminal

InterPro entry
Short nameLI-POR_suB-like_C
Overlapping
homologous
superfamilies
 

Description

This domain is found in Light-independent protochlorophyllide reductase subunit B (LI-POR subunit B, also known as DPOR subunit B) and similar bacterial and plant chloroplast proteins. It often appears at the C-terminal of nitrogenase component 1 type oxidoreductases (
IPR000510
) and sometimes independently in certain bacterial proteins such as the Protochlorophyllide reductase BchB subunit of the cyanobacterium Synechocystis.

LI-POR subunit B is a component of the dark-operative protochlorophyllide reductase (DPOR), a nitrogenase-like metalloenzyme that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide), leading to the specific architecture of chlorophylls. The X-ray crystallographic structure of this complex from the marine cyanobacterium Prochlorococcus marinus showed that the C-terminal domain of subunit B closes the substrate-binding cavity at the interface with the other component of the complex, possibly preventing the organism from Pchlide-induced photodynamic damage
[1]
.

This domain is also associated with chlorophyllide reductase subunit Z, which converts chlorophylls (Chl) into bacteriochlorophylls (BChl) by reducing ring B of the tetrapyrrole
[2]
.

References

1.Structure of ADP-aluminium fluoride-stabilized protochlorophyllide oxidoreductase complex. Moser J, Lange C, Krausze J, Rebelein J, Schubert WD, Ribbe MW, Heinz DW, Jahn D. Proc Natl Acad Sci U S A 110, 2094-8, (2013). PMID: 23341615

2.A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus. Nomata J, Mizoguchi T, Tamiaki H, Fujita Y. J Biol Chem 281, 15021-8, (2006). PMID: 16571720

GO terms

Cross References

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