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chlL-A

Gene
chlL-A
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Chaetosphaeridium globosum
Length
290 amino acids
Function
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
Similarity
Belongs to the NifH/BchL/ChlL family.
Mass
31.794 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAESQESLNYVCDFYLNIADQILSCPEGVVPKEVPDRELFSLLSDFYLNPTLSEKENTLSPSSLDFMMV

Gene
chlL-A
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Chaetosphaeridium globosum
Length
290 amino acids
Function
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
Similarity
Belongs to the NifH/BchL/ChlL family.
Mass
31.794 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAESQESLNYVCDFYLNIADQILSCPEGVVPKEVPDRELFSLLSDFYLNPTLSEKENTLSPSSLDFMMV