Literature summary for 1.3.7.7 extracted from

Nomata, J.; Terauchi, K.; Fujita, Y.
Stoichiometry of ATP hydrolysis and chlorophyllide formation of dark-operative protochlorophyllide oxidoreductase from Rhodobacter capsulatus (2016), Biochem. Biophys. Res. Commun., 470, 704-709 .

Search for more literature for 1.3.7.7

Organism

Organism	UniProt	Comment	Textmining
Rhodobacter capsulatus	D5ANS3 and P26164 and P26163	D5ANS3 i.e. iron-sulfur ATP-binding protein BchL, P26164 i.e. subunit BchN, P26163 i.e. reductase subunit BchB	-
Rhodobacter capsulatus ATCC BAA-309	D5ANS3 and P26164 and P26163	D5ANS3 i.e. iron-sulfur ATP-binding protein BchL, P26164 i.e. subunit BchN, P26163 i.e. reductase subunit BchB	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O	-	Rhodobacter capsulatus	chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate	-	?
protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O	-	Rhodobacter capsulatus ATCC BAA-309	chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate	-	?

Synonyms

Synonyms	Comment	Organism
bchB	-	Rhodobacter capsulatus
bchL	-	Rhodobacter capsulatus
bchN	-	Rhodobacter capsulatus
dark-operative protochlorophyllide oxidoreductase	-	Rhodobacter capsulatus
DPOR	-	Rhodobacter capsulatus

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Release 2023.1 (January 2023)