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chlL

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Auxenochlorella protothecoides
Length
300 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
32.843 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQAKDYHYEDVWPEDVIYQGYGEVDSVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIVASVREKSKTHPLRLAGLIGNRTSKRDLIDKYVEVCPMPVIEVLPLIEDIRVSRVKGKTVFEMAETDQKLNYICDFYLNIADQLLASPEGVIPLELEDRELFTLLSTFYLTVTPQNQGETQSTISTPLTSNSASELDFILV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Chlorella vulgaris
Length
300 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
32.843 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQAKDYHYEDVWPEDVIYQGYGEVDSVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIVASVREKSKTHPLRLAGLIGNRTSKRDLIDKYVEVCPMPVIEVLPLIEDIRVSRVKGKTVFEMAETDQKLNYICDFYLNIADQLLASPEGVIPLELEDRELFTLLSTFYLTVTPQNQGETQSTISTPLTSNSASELDFILV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Auxenochlorella protothecoides
Length
300 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
32.843 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQAKDYHYEDVWPEDVIYQGYGEVDSVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIVASVREKSKTHPLRLAGLIGNRTSKRDLIDKYVEVCPMPVIEVLPLIEDIRVSRVKGKTVFEMAETDQKLNYICDFYLNIADQLLASPEGVIPLELEDRELFTLLSTFYLTVTPQNQGETQSTISTPLTSNSASELDFILV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Chlorella vulgaris
Length
300 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
32.843 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQAKDYHYEDVWPEDVIYQGYGEVDSVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIVASVREKSKTHPLRLAGLIGNRTSKRDLIDKYVEVCPMPVIEVLPLIEDIRVSRVKGKTVFEMAETDQKLNYICDFYLNIADQLLASPEGVIPLELEDRELFTLLSTFYLTVTPQNQGETQSTISTPLTSNSASELDFILV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechococcus sp. (strain RCC307)
Length
300 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
32.898 kDa
Sequence
MTTTLTPPSSRREDGDGSVQVHQDASLKIEEGALVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELQPEDFVFEGFNGVMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVQAIQAKAKNYKVRLGGVVANRSAETDQIDKFNERTGLRTMAHFRDVDAIRRSRLKKCTIFEMDKDEEGVEAVQNEYLLLAQNMLDHVEPLEAESLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Chlorokybus atmophyticus
Length
296 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
32.402 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRISRVKGKTLFEMAESEPSLDYVCEFYLNIADQLLARPEGVVPKEVPDRELFSLLSDFYLNPANNASSIEQPTDSIVQSEQEPFLII

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Chlorokybus atmophyticus
Length
296 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
32.402 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRISRVKGKTLFEMAESEPSLDYVCEFYLNIADQLLARPEGVVPKEVPDRELFSLLSDFYLNPANNASSIEQPTDSIVQSEQEPFLII

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechococcus sp. (strain CC9605)
Length
296 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
32.467 kDa
Sequence
MTTILTRPADGEGSVQVHQDPALNIQEETLVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELRPEDFVFTGFNGVQCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVQAIQAKAKNYKVRLGGVVANRSADTDQIDKFNERTGLRTMAHFRDVDAIRRSRLKKCTIFEMDDADEAVQAVQNEYLRLAQNMLDKVEPLEATSLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Length
296 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
32.395 kDa
Sequence
MTTTLANRPDGEGSVQVKLDPKVNIEEGALVIAVYGKGGIGKSTTSSNLSAAFSKLGKKVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELRPQDFMFEGFNGVQCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVAAINAKAKNYKVRLGGVIANRSAELDQIEKFNEKTGLKTMAHFRNVDAIRRSRLKKCTIFEMDPEEEGVLEVQNEYLSLAKKMIDNVEPLEAEPLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Prochlorococcus marinus (strain MIT 9313)
Length
296 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
32.341 kDa
Sequence
MTTTLTRPADGEGSVQVQQDASVRIQEGALVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTHRMVPTVIDILEEVDFHSEELRPDDFMFEGFNGVKCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVAAINAKAKNYKVRLGGVIANRSAELDQIEKFNQQTGLKTMAHFKNVDAIRRSRLKKCTIFEMDSSDEGVMECQNEYLSLAQKMLDNVEPLEAEPLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Prochlorococcus marinus (strain NATL2A)
Length
296 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
32.464 kDa
Sequence
MTSTITRKEDGEGSVQVKQDPKAQIQEGALVIAVYGKGGIGKSTTSSNLSAAFSKLGKKVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELRPEDFMFKGFNGVMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVAAINAKAKNYKVRLGGVIANRSAELDQIEKFNERTGLKTMAHFRNVDAIRRSRLKKCTIFEMDSEEEGVVEVQNEYLSLAQKMIDNVEPLEAEPLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechococcus sp. (strain WH7803)
Length
296 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
32.546 kDa
Sequence
MTTTLKRPTDGEGSVQVHQDPSVNIEEETLVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELRPEDFVFSGFNGVQCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVQAIQAKAKNYKVRLGGVVANRSADTDQIDKFNERTGLRTMAHFKDVDAIRRSRLKKCTIFEMDDDDEAVQAVREEYLRLAQNMLDNVEPLEATSLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechococcus sp. (strain WH8102)
Length
296 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
32.502 kDa
Sequence
MTTTLTRPTDGEGSVQVHQDPGLNIQEETLVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELRPEDFVFTGFNGVQCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVQAIQAKAKNYKVRLGGVVANRSADTDQIDKFNERTGLRTMAHFKDVDAIRRSRLKKCTIFEMDDEDEAVQAVRSEYLRLAQNMLDKVEPLEATSLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechococcus sp. (strain CC9311)
Length
296 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
32.334 kDa
Sequence
MTTTLTRPADGDGSVQVHQDPGTKIEEGALVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELRPEDFMFTGYNGVKCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVQAIQAKAKNYKVRLGGVVANRSAETDQIDKFNERTGLRTMAHFKDVDAIRRSRLKKCTIFEMDDKDDGVKAVQDEYIRLASNMLNNVEPLEAVSLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechococcus sp. (strain CC9902)
Length
296 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
32.37 kDa
Sequence
MTTTLSRPTDGEGSVQVQQDPSMKIEEGALVIAVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTHSMVPTVIDILEEVDFHSEELRPDDFVFTGYNGVKCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVQAIQAKAKNYKVRLGGVIANRSADTDQIDKFNERTGLRTMAHFKDVDAIRRSRLKKCTIFEMDDDDDAVKAVKNEYLRLAQNMLDNVEPLEAVSLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Prochlorococcus marinus (strain MIT 9515)
Length
295 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
32.319 kDa
Sequence
MTSTINKHLDGEGSVQVKQDPKVNIEEGALVIAVYGKGGIGKSTTSSNLSAAFSKLGKKVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELRPTDFMFEGFNGVMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVSAIKAKAKNYKVRLGGVVANRSKDTDQIDKFNDRTGLKTMAHFKDVDAIRRSRLKKCTIFEMEPTEDVIEVQNEYLSLAKNMLENVEPLEGTPLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Prochlorococcus marinus (strain MIT 9312)
Length
295 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
32.32 kDa
Sequence
MTSTINKPLDGEGSVQVKQDPKINIEEGALVIAVYGKGGIGKSTTSSNLSAAFSKLGKKVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELRPTDFMFEGFNGVMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVSAIKAKAKNYKVRLGGVVANRSKDTDQIDKFNERTGLKTMAHFKDVDAIRRSRLKKCTIFEMEPTEDVIEVQNEYLSLAKNMLENVEPLEGNPLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4)
Length
295 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
32.25 kDa
Sequence
MTSTINKPLDGEGSVQVKQDPKVNIEEGALVIAVYGKGGIGKSTTSSNLSAAFSKLGKKVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELRPTDFMFEGFNGVMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVSAIQAKAKNYKVRLGGVVANRSKDTDQIDKFNNRTGLKTMAHFKDVDAIRRSRLKKCTIFEMEPTEDVVEVQNEYLSLAKNMLDNVEPLEGTPLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Prochlorococcus marinus (strain AS9601)
Length
295 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
32.348 kDa
Sequence
MTSTINRPLDGEGSVQVKQDPKINIEEGALVIAVYGKGGIGKSTTSSNLSAAFSKLGKKVLQIGCDPKHDSTFTLTHKMVPTVIDILEEVDFHSEELRPTDFMFEGFNGVMCVESGGPPAGTGCGGYVTGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHANYCLIVTANDFDSIFAMNRIVSAIKAKAKNYKVRLGGVVANRSKDTDQIDKFNERTGLKTMAHFKDVDAIRRSRLKKCTIFEMEPTEDVIEVQNEYLSLAKNMLENVEPLEGNPLKDREIFDLLGFD

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Adiantum capillus-veneris
Length
293 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
32.23 kDa
Sequence
MKVAVYGKGGIGKSTTSCNISIALARRGRKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQVKDYHYEDVWPEDVIYRGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKSHTHPLRLAGLVGNRTSGRDLIDKYVEACPMPVLEVLPLVEDIRVSRVKGKTLFEMAEYQPNLNYVCDFYLNIADQILSEPEGVVPREIPDRELFSLLSDFYLNSTFTNESDGGYDHQDVPLDFTII

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Chlamydomonas reinhardtii
Length
293 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
31.945 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISIALRKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLSSKDYHYEDIWPEDVIYGGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFFEYDVILFDVLGDVVCGGFAAPLNYADYCIIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTSKRDLIDKYVEACPMPVLEVLPLIEEIRISRVKGKTLFEMSNKNNMTSAHMDGSKGDNSTVGVSETPSEDYICNFYLNIADQLLTEPEGVIPRELADKELFTLLSDFYLKI

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Adiantum capillus-veneris
Length
293 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
32.23 kDa
Sequence
MKVAVYGKGGIGKSTTSCNISIALARRGRKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQVKDYHYEDVWPEDVIYRGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKSHTHPLRLAGLVGNRTSGRDLIDKYVEACPMPVLEVLPLVEDIRVSRVKGKTLFEMAEYQPNLNYVCDFYLNIADQILSEPEGVVPREIPDRELFSLLSDFYLNSTFTNESDGGYDHQDVPLDFTII

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Chlamydomonas reinhardtii
Length
293 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
31.945 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISIALRKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLSSKDYHYEDIWPEDVIYGGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFFEYDVILFDVLGDVVCGGFAAPLNYADYCIIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTSKRDLIDKYVEACPMPVLEVLPLIEEIRISRVKGKTLFEMSNKNNMTSAHMDGSKGDNSTVGVSETPSEDYICNFYLNIADQLLTEPEGVIPRELADKELFTLLSDFYLKI

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Huperzia lucidula
Length
292 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
32.314 kDa
Sequence
MKLAIYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQIKDYHYEDVWPEDVIHKGYGGVDRVEAGGPPAGAGCGGYVVGETVKLSKELNAFYEYDIILFDVLGDAVRGGFASPLNYADYCIIIADNGFDALLATNRIAASVREKARTRTHPLRLAGLVGNRTSERDLIDKYVEVCPMPILEILPLIEDIRVSRIKGKTLFEMVESQPYLNYVCDFYLNTADQILSKPEGIIPKEISDRELFSLLSDFYLNPVGNEEQENKENLLDSVVLI

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Huperzia lucidula
Length
292 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
32.314 kDa
Sequence
MKLAIYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQIKDYHYEDVWPEDVIHKGYGGVDRVEAGGPPAGAGCGGYVVGETVKLSKELNAFYEYDIILFDVLGDAVRGGFASPLNYADYCIIIADNGFDALLATNRIAASVREKARTRTHPLRLAGLVGNRTSERDLIDKYVEVCPMPILEILPLIEDIRVSRIKGKTLFEMVESQPYLNYVCDFYLNTADQILSKPEGIIPKEISDRELFSLLSDFYLNPVGNEEQENKENLLDSVVLI

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Larix decidua
Length
291 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
31.809 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISVALARRGQKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDIWPEDVIHKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCVIITDNGFDALFAANRITASIREKARTHPLRLAGLVGNRTSKRDLIHKYVEACPMPVIEVLPIIEDIRVSRVKGKTLFEMVGSEPSLNYVCKYYLDIADQILSQPEGIVPKEIPDRELFSLLSDLYLNPIGGGGQKKKNQENLLGFTRI

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Larix decidua
Length
291 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
31.809 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISVALARRGQKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDIWPEDVIHKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCVIITDNGFDALFAANRITASIREKARTHPLRLAGLVGNRTSKRDLIHKYVEACPMPVIEVLPIIEDIRVSRVKGKTLFEMVGSEPSLNYVCKYYLDIADQILSQPEGIVPKEIPDRELFSLLSDLYLNPIGGGGQKKKNQENLLGFTRI

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Angiopteris evecta
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
31.856 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKSLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKAHTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAESQPTLNYVCEFYLNIADQILSQPEGVVPKEIPDRELFSLLSDFYLNPINSGKNENIENNLHDFMII

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Anthoceros angustus
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
32.064 kDa
Sequence
MKIAVYGKGGIGKSTTSCNTSIASARRGKRVLQIGCDPKHDSTFTLTGSLIPTIIDTSQSKDYHYEDVWPEDVIYKGYGGVDCVEVGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVSGDVVCGGFVVLLNYADYCIIITDNGFDALFAVNCIAASVREKARTHSLRLAGSVGNRTSKRDLINRYVEACPMPVLEVSLLIEDIRVSRVKGKTSFEMVEFQPFLNYVCEFYLNIADQILSQPEGVIPKEIPDRELFSLLSDFYLNPTNNERENKNQETLLDFMII

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Cycas taitungensis
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
31.553 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGGKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEEIWPEDVIHKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGLAAPLNYADYCVIITDNGFDALFAANRIAVSIGEKTRTHLLRLAGLVGNRTSKRDLIDGYVEVCPMPVIEVLPLIEDIRISRVKGKTLFEMVGSEPSLNYVCEYYLNIADQILSQPEGIVPKEIPDRKFFSLLSDSYLSPINDGKQGKNQENLLGFTMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Angiopteris evecta
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
31.856 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKSLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKAHTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAESQPTLNYVCEFYLNIADQILSQPEGVVPKEIPDRELFSLLSDFYLNPINSGKNENIENNLHDFMII

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Anthoceros angustus
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
32.064 kDa
Sequence
MKIAVYGKGGIGKSTTSCNTSIASARRGKRVLQIGCDPKHDSTFTLTGSLIPTIIDTSQSKDYHYEDVWPEDVIYKGYGGVDCVEVGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVSGDVVCGGFVVLLNYADYCIIITDNGFDALFAVNCIAASVREKARTHSLRLAGSVGNRTSKRDLINRYVEACPMPVLEVSLLIEDIRVSRVKGKTSFEMVEFQPFLNYVCEFYLNIADQILSQPEGVIPKEIPDRELFSLLSDFYLNPTNNERENKNQETLLDFMII

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Cycas taitungensis
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
31.553 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGGKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEEIWPEDVIHKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGLAAPLNYADYCVIITDNGFDALFAANRIAVSIGEKTRTHLLRLAGLVGNRTSKRDLIDGYVEVCPMPVIEVLPLIEDIRISRVKGKTLFEMVGSEPSLNYVCEYYLNIADQILSQPEGIVPKEIPDRKFFSLLSDSYLSPINDGKQGKNQENLLGFTMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Zygnema circumcarinatum
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
31.832 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAESEPSLNYVCEFYLNIADQILSQPEGVVPKEVPDRELFSLLSDFYLNPSSSRSDMQLEDNSLDFVMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Pyropia yezoensis
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
31.879 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALSKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDIILFDVLGDVVCGGFAAPLNYADYCLIITDNGFDALFAANRIAASVREKARTHSLRLAGLVGNRTDKRDLIDKYIDCVPMPVLEVLPLIEDIRVSRVKGKTLFEMAEIDKDLAYVCDYYLNIADQLITRPEGVVPKESPDRELFSLLSDFYLNPKSKVGQEKVDQEELDLMIV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Cyanothece sp. (strain PCC 8801)
Length
289 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
31.661 kDa
Sequence
MTLTLAVYGKGGIGKSTTSCNISTALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDFHYEDIWPEDVIYKGYAGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTSKRDLIDKYIEAVPMPVLEILPLIEDIRVSRVKGKTLFEMTESDPSLDYVCNYYLNIADQLLAMPEGVVPNDAPDRELFTLLSDFYLNPQTPVKSQEEELDLMMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Cyanothece sp. (strain PCC 8801)
Length
289 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
31.661 kDa
Sequence
MTLTLAVYGKGGIGKSTTSCNISTALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDFHYEDIWPEDVIYKGYAGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTSKRDLIDKYIEAVPMPVLEILPLIEDIRVSRVKGKTLFEMTESDPSLDYVCNYYLNIADQLLAMPEGVVPNDAPDRELFTLLSDFYLNPQTPVKSQEEELDLMMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Tetradesmus obliquus
Length
289 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
31.812 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISIALAKRGKKVLQIGCDPKSDSTFTLTGFLIPTIIDTLQAKDYHYEDVWPEDVIYQGYAGVDCVEAGGPPAGAGCGGYVVGETVKLLKEFNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIVTDNGFDALFAANRITASVREKARTHPLRLAGLIGNRTKKRDLIEKYVETCPMPILEVLPLIEDIRVSRVKGKTLFEMTESEPTLQFVCDFYLNIADQLLTQPEGVIPRELGDRELFNLLSNFYLNSSNSTNTTLKNETNLFDLV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Staurastrum punctulatum
Length
289 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
31.678 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGKRVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAESDPSQNYVCDFYLNIADQILSKSEGVVPREVPDRELFSLLSDFYLNQPSSSTNNSETNNLDFLMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Length
288 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
31.449 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCMIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTSKRDLIEKYVEAVPMPVLEVLPLIEDIRVSRVKGKTLFEMAESDPSLNYVCDYYLSIADQILARPEGVVPNDAPDRELFSLLSDFYLNPGKPQVPNPEEELDLMIV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Chara vulgaris
Length
288 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
31.729 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGEVNCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETDSSLEYVCDYYLNIADQILSQPEGIVPKEIPDRELFTLLSDFYLNININSNNLEKNESSFLII

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Length
288 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
31.449 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCMIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTSKRDLIEKYVEAVPMPVLEVLPLIEDIRVSRVKGKTLFEMAESDPSLNYVCDYYLSIADQILARPEGVVPNDAPDRELFSLLSDFYLNPGKPQVPNPEEELDLMIV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Chara vulgaris
Length
288 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
31.729 kDa
Sequence
MKIAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDVWPEDVIYKGYGEVNCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDVILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKARTHPLRLAGLVGNRTSKRDLIDKYVEACPMPVLEVLPLIEDIRVSRVKGKTLFEMAETDSSLEYVCDYYLNIADQILSQPEGIVPKEIPDRELFTLLSDFYLNININSNNLEKNESSFLII

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
288 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
31.48 kDa
Sequence
MTLTLAVYGKGGIGKSTTSCNISTALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDFHYEDIWPEDVIYKGYAGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAAKRIAASVREKARTHSLRLAGLIGNRTSKRDLIDKYIEAVPMPVLEILPLIEDIRVSRVKGKTLFEMAESDPSLNYVCDYYLNIADQILSQPEGVVPKDAQDRDLFSLLSDFYLNPTQPASQTKELDLMMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Trichodesmium erythraeum (strain IMS101)
Length
288 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
31.54 kDa
Sequence
MKLSVYGKGGIGKSTTSCNISVALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDYHYEDIWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYSDYCMIVTDNGFDALFAANRIAASVREKARTHTLRLAGLIGNRTSKRDLINKYVEAVPMPVLEVLPLIEDIRVSRVKGKTLFEMAETDPSLQYVCNYYLNIADQILALPEGVVPSESPDRDLFALLSDFYLNPSKSHVMSEDEELDLMMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Stigeoclonium helveticum
Length
288 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
31.706 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQAKDYHYENVWPEDVIYQGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIAASVREKARTHPLRLAGLVANRTTKRDLIDKYVQVCPIPVLEVLPLLEDIRVSRVKGKTLFEMAESEPDLSFVLDYYLNIADQLLTEPEGVVPRELGDRELFSLLSDFYLNIENQTSVNKTEKLDFFLV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6)
Length
288 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
31.437 kDa
Sequence
MTMTLAVYGKGGIGKSTTSCNISVALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDFHYEDIWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTSKRDLIEKYVSHVPMPVLEVLPLIEDIRVSRVKGKTLFEMAEGDSMLDYVCDFYLNIADQVLAAPEGVVPSEASDRELFSLLSDYYLNPPVEKTQEDELDLMMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Acaryochloris marina (strain MBIC 11017)
Length
286 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
31.258 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDYHYEDVWPEDVIYKGFGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCMIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTSKRDLIDKYIDSVPMPVLEILPLIEDIRVSRVKGKTMFEMAESDPSLEPVCNYYLNIADQILAGPEGVVPEDAQDRELFALLSDFYLNPTQPKTEEEELDLMMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
Length
286 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
31.193 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYENVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIAASVREKARTHVLRLAGLIGNRTAKRDLIDKYVEAVPMPVLEILPLIEDIRVSRVKGKTLFEMAESDPSLNYVCDYYLNIADQILARPEGVVPQGAPDRDLFALLSDFYLNPAPNKVEQEDLELMMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Leptolyngbya boryana
Length
286 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
31.22 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDYHYEDVWAEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCMIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTAKRDLIEKYVDAVPMPILEVLPLIEDIRVSRVKGKTLFEMAESDPSLNYVCDYYLNIADQILANPEGVVPKDAADRDLFSLLSDFYLNPQQPKTAEEELDLMMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Acaryochloris marina (strain MBIC 11017)
Length
286 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
31.258 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDYHYEDVWPEDVIYKGFGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCMIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTSKRDLIDKYIDSVPMPVLEILPLIEDIRVSRVKGKTMFEMAESDPSLEPVCNYYLNIADQILAGPEGVVPEDAQDRELFALLSDFYLNPTQPKTEEEELDLMMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
Length
286 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
31.193 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYENVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIAASVREKARTHVLRLAGLIGNRTAKRDLIDKYVEAVPMPVLEILPLIEDIRVSRVKGKTLFEMAESDPSLNYVCDYYLNIADQILARPEGVVPQGAPDRDLFALLSDFYLNPAPNKVEQEDLELMMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Leptolyngbya boryana
Length
286 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
31.22 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDYHYEDVWAEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCMIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTAKRDLIEKYVDAVPMPILEVLPLIEDIRVSRVKGKTLFEMAESDPSLNYVCDYYLNIADQILANPEGVVPKDAADRDLFSLLSDFYLNPQQPKTAEEELDLMMV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechococcus elongatus (strain PCC 7942)
Length
286 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
31.118 kDa
Sequence
MKLSVYGKGGIGKSTTSCNISVALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQAKDYHYEDVWPEDVIYRGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYSDYCLIITDNGFDALFAANRIAASVREKARTHTLRLAGLIGNRTSKRDLIDKYIEAVPMPVLEVLPLIEDIRISRVKGKTVFEMAETEPSLLTVCDYYLNIADQILARPEGVVPKDAADRDLFSLLSDFYLNPPKQTTEAIAPEALLV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Length
286 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
31.118 kDa
Sequence
MKLSVYGKGGIGKSTTSCNISVALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQAKDYHYEDVWPEDVIYRGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYSDYCLIITDNGFDALFAANRIAASVREKARTHTLRLAGLIGNRTSKRDLIDKYIEAVPMPVLEVLPLIEDIRISRVKGKTVFEMAETEPSLLTVCDYYLNIADQILARPEGVVPKDAADRDLFSLLSDFYLNPPKQTTEAIAPEALLV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechococcus sp. (strain JA-3-3Ab)
Length
283 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
30.806 kDa
Sequence
MEERAVKLAVYGKGGIGKSTTSCNLSVALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLEAKGYHYEDIYPEDVIYRGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCVIVTDNGFDALFAANRIAASVREKAKTRKLRLAGLIGNRTSKRDLIDQYVSAVPMPVLEVLPLVEDIRISRVKGKTLFEMAETDPSLEPVCQYYLNIADELLARPEGIVPRPAEDRELFALLSDFYKTPVREPALV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Synechococcus sp. (strain JA-2-3B'a(2-13))
Length
283 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
30.767 kDa
Sequence
MEERAVKLAVYGKGGIGKSTTSCNISVALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLEAKGYHHEDIYPEDVIYRGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIAASVREKAKTRKLRLAGLIGNRTSKRDLIDKYVSAVPMPVIEVLPLIEDIRVSRVKGKTLFEMAETDPSLEPVCQYYLNIADELLARPEGIVPQPAEDRELFALLSDFYNTPARQLALV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Cyanophora paradoxa
Length
282 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
30.847 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALAKRGKKVLQIGCDPKHDSTFTLTGHLIPTIIDTLQEKDFHYEDIWPEDVIYKGYAGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDIILFDVLGDVVCGGFASPLNYADYCLIVTDNGFDALFAANRIAASVREKARTHQLRLAGLIGNRTTKSDLIEKYTENVPIPILQLLPLIEDIRISRVKGKTLFEMSESNPELSPICDYYLNIADQILAKPEGIIPNEVLDRDLFTLLSDFYLNMDSSESSNLTLV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Cyanophora paradoxa
Length
282 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
30.847 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALAKRGKKVLQIGCDPKHDSTFTLTGHLIPTIIDTLQEKDFHYEDIWPEDVIYKGYAGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDIILFDVLGDVVCGGFASPLNYADYCLIVTDNGFDALFAANRIAASVREKARTHQLRLAGLIGNRTTKSDLIEKYTENVPIPILQLLPLIEDIRISRVKGKTLFEMSESNPELSPICDYYLNIADQILAKPEGIIPNEVLDRDLFTLLSDFYLNMDSSESSNLTLV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Thermosynechococcus elongatus (strain BP-1)
Length
281 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
30.542 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALARRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQAKDYHYEDVWPEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCLIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTNKRDLIEKYVEAVPMPILEVLPLIEDIRVSRVKGKTLFEMAESDPSLNDVCDYYLNIADQILARPEGVVPKDVPDRDLFALLSDFYLNPQGSERSLAAV

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)
Length
275 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
29.996 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALAKRGRRVLQIGCDPKHDSTFTLTGFLIPTIIDTLEEKDYHYEDVYAEDVIYEGYGGVHCVEAGGPPAGAGCGGYVVGETMKLLKELRAFEDHDVILFDVLGDVVCGGFAAPLNYADYCVIITDNGFDALFAANRIAASCREKARTHPLKLAGLVGNRTNKRDLIDKYVEAVPMPVLEILPLIEDIRVSRVKGKTIFEMAETDPSLEPVCQYYLNIADHLLACPEGVVPQECPDRALFELLSDFYSRTPVPA

Gene
chlL
Protein
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Organism
Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)
Length
275 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
29.996 kDa
Sequence
MKLAVYGKGGIGKSTTSCNISVALAKRGRRVLQIGCDPKHDSTFTLTGFLIPTIIDTLEEKDYHYEDVYAEDVIYEGYGGVHCVEAGGPPAGAGCGGYVVGETMKLLKELRAFEDHDVILFDVLGDVVCGGFAAPLNYADYCVIITDNGFDALFAANRIAASCREKARTHPLKLAGLVGNRTNKRDLIDKYVEAVPMPVLEILPLIEDIRVSRVKGKTIFEMAETDPSLEPVCQYYLNIADHLLACPEGVVPQECPDRALFELLSDFYSRTPVPA