About Products Protein Database Contact

ndhB

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Length
534 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
57.075 kDa
Sequence
MDFANIASQLNAGTILPEGIVILTLLGVLIVDLILGRTSARWIGYLAIAGLFTSIVALYFQWDNPNPISFTGGFNGDDLSIVFRGIIALSAAVTILMSIRYVDQSGTPLAEFIAILLSATLGGMFLSGASELVMIFISLETLSISSYLLTGYTKRDPRSNEAALKYLLIGASSTAVFLYGVSLLYGLSGGQTELSAIANGIATAKVGQSLGLVIALVFAIAGIGFKISAAPFHQWTPDVYEGAPTPVIAFLSVGSKAAGFALAIRLLTTAFPLVADEWRFVFTALAVLSMILGNVVALAQTSMKRMLAYSSIAQAGFVMIGLIAGTQAGYASMIFYLLVYLFMNLCGFTCIILFSLRTGTDQIAEYSGLYQKDPLLTLGLSIALLSLGGIPPLAGFFGKIYLFWAGWQAGLYWLVLLGLVTTVVSIYYYIRVVKMMVVKEPHEMSDAVKNYPQVRWDLPGLRPLQVGLVITLIATSLAGILSNPLFTLANNSISNTPFLQATINSHVEAQNLLLLPKLDSVSQSQPSVDSTAKI

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Synechococcus sp. (strain JA-2-3B'a(2-13))
Length
527 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.672 kDa
Sequence
MDVFAPTGNLYAGAIWPEVVVTLTLLLVLVVDLVGGSAARKSLPALSIFGLIGALVTLVLQWQQPQLESFLGSFAADPVSILFRGLVVGTAVLTVMMAERYIAQSGAPTGEFYVLLLTATLGGMFLSGATDLILVFVSLETLGIASYLMAGYTKRDPRSSEAALKYLLIGASSTAIFLYGMSLLYGLSGGQTKLEAIASSMGDAGLAGIIALVLCIGGIGFKLAAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAVRFLATVFPAMTEEWRAVLSVLAILTMVLGNVVAIAQTRLKRLLAYSSIGQAGFVMIGLVVGTEAGYASLIFYLLVYLVMNLGAFLCITLFSLKTGTDEINEYSGLYQKDPFLTLCLSICLLSLGGLPPLAGFFGKLYLFWAGWQAGAYTLVLVGLVTSVISIYYYVRVVKTIVVKEPQEMSVSVQNYPETNWQAEGMPALRVGMVLTLVATIFAGILSNPLFTLSIQAVEQSPFLGFPTAQAPIPESASLQVAVDGSLGSLTQPSQG

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6)
Length
526 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.148 kDa
Sequence
MDFSSTVASQLYTGAILPESIVILTLIVVLVGDLIVGRARSGWIPYAAIAGLLGSVFALYLGWDNPHPVAFLGAFNSDNLSILFRGIIVLSTAFTIMMSVRYVERSGTALSEFICILLTATLGGMFLSGANELVMIFVSLEMLSISSYLLTGYMKRDPRSNEAALKYLLIGAASSAIFLYGVSLLYGLSGGKTILSEIALGFTDPQGGQSLALAIALVFAIAGIAFKISAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRLLVTVFNPVSEEWHFIFTALAILSMVLGNVVALAQTSMKRMLAYSSIAQAGFVMIGLVAGTDAGYSSVIFYLLVYLFMNLGAFTCVILFSLRTGTDQIAEYAGLYQKDPLLTLGLSVCLLSLGGIPPLAGFFGKIYLFWAGWQAGLYGLVLLGLITSVISIYYYIRVIKMMVVKEPQEMSDSVRNYPAVTWTAVGMKPLQVGLVLSVIITSLAGILSNPLFVIADQSVTSTPMLQVANHPTEQVVAQVDSELVGVAIADH

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Trichodesmium erythraeum (strain IMS101)
Length
526 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.002 kDa
Sequence
MIDLSTIAAQLNARTILPEGIVVITLLVVLVGDLILGRSSTKWTPYAAIVGLLGAIVALYTQWDSSNTIGFLGAFNADALSIAFRGIIAISAITTILMSVAYIEQTGTPLGEFICILLTATLGAMFLSGADELVMIFISLETLSISSYLLTGYTKRDPRSNEAALKYLLIGAASSAIFLYGISLLYGLSGGETRLTAIASSMANAGSANISLALVIALVFAIAGISFKISAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRLLVTAFPLVSEQWHFVFTALAILSMVLGNVVALAQTSMKRLLAYSSIGQAGFVMIGLLANTEAGYASMIFYLLVYLFMNLGGFTCVILFSLRTGTDQISEYAGLYQKDPLLTLGLSLCLLSLGGIPPLAGFFGKIYLFWAGWQAGLYWLVLLGLITSVASIYYYIRVVKMMVVKEPQEMSDVIKNYPPISWKLPGMRPLQVGLILSVLATSLAGILSNPLFTLANSSIAKTPMLNSALVKTVEANSVASQLDFSLPSKN

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Synechococcus sp. (strain JA-3-3Ab)
Length
525 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.363 kDa
Sequence
MDVFAPTGNLHAGAIWPEVVVTLTLLIVLVVDLVGGSAARKSLPALSLFGLLGALVTLVLQWQQPQLESFLGSFAADPVSILFRGLVVATAALTVMMAERYFLQAGAPTGEFYVLLLTATLGGMFLAGATDLIMVFVSLETLGIASYLMAGYTKRDPRSSEAALKYLLTGASSTAIFLYGMSLLYGLSGGQTQLAAIAPYLANAGLVGILALVFCLGGIGFKLAAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRFLATVFPAMTEEWRAVLSVLAILTMVLGNVVAIAQTRLKRLLAYSSIGQAGFVLIGLVAGTEAGYASLIFYLMVYLAMNLGAFLCVTLFSLKTGTDEINEYSGLYQKDPFLTLCLSICLLSLGGLPPLAGFFGKLYLFWAGWQAGEYTLVLVGLVTSVISIYYYVRVVKTMVVKEPQEMSLSVQNYPPTDWQAEGMPALRVGMVVTLVATIFAGILSNPLFTLSTQAVEQSPFLGFPTAQAFAPGSASPSLAVAGSAALPSRGS

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Length
524 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.319 kDa
Sequence
MPDMGTPLLTIQGMASPGELLNLSLNAKAILPEGFVLLALIGTLLVDLAGEEISKRWSPPICYAGLGSALIILGFGWNQSPESAFLGAFIADNFSIAFRAVVALSTLISLLISWRYAEQSGSPVGEYAAILLAATLGAMLLCGSTDLISIFISLETLSVASYLLAGYLKRDARSSEAALKYLLVGSAAAAVFLYGASLLYGLSGSTSLESIGIALQTSPTPLAALALVFILATVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAVRILVGCFNAFDDQWKLLFTVLAVLSMTLGNVVALAQTSMKRMLAYSSIGQAGFVMIGLVCGTEEGYAAMILYMAAYLFMNLGAFACIILFSLRTGSDRIADYAGLYQKDPLITLGLSLCLLSLGGIPPMLGFFGKIYLFFAGWSDGQYLLVIVGLVTSVVSIYYYISVIKMMVVKEPQEASELVKAYPLIQWNSIGMPTLRFALLTCVFATAIGGVLSNPLFKWANSAVAGTPLLQEALTLAAEKGAIG

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Synechococcus sp. (strain WH7803)
Length
523 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.643 kDa
Sequence
MPEMGALLLTTPALAAPGELLNLSLNASAVAPEGAVLLAMLATLLVDLAGEKVSTRWVPPICYAGLGTALLLLALQWNAPLEPSFLGAFLPDHLAIAFRAVVALSTLLSLMISWRYAEQGGTPVGEYAGILLAATLGGMLLCGATDLVSVFVSLETLSVASYLLSGYMKRDARSSEAALKYLLVGSAAAAVFLYGSSLLYGLSGSTSLEAIGQALLSSPTPLAALALVFVLATVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALALRLLVGCFGSFDTQWKLLFTVLAVLSMTLGNVVALAQTSMKRMLAYSSIGQAGFVMIGLVCGTEDGFAAMVLYTAAYLFMNLGAFACIILFSIRTGSDRIADYAGLYQKDPLITLGLSLCLLSLGGIPPMLGFFGKIYLFFAGWADHQYVLVVVGLITSVISIYYYIGVIKMMVVKEPQEASDAVKAYPPVQWSTLGLPPLRVALVTCVVVTAVGGILSNPLFQWASDAVAGTPLLQQAIASVNGSSLG

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Synechococcus sp. (strain WH8102)
Length
523 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.893 kDa
Sequence
MPEMGVFLLAAQAMAAPGELLNLSLNATAVLPEGAVLLAMIATLLVDLAGEKVAARWVPPICYGGLGTALVLLALQWNAPVESSFLGAFLADNLAVAFRAVIALSTLLSLLISWRYAEQSGTPVGEFAAILLAATLGAMLLCGATDLVSVFISLETLSVASYLLSGYMKRDARSSEAALKYLLVGSAAAAVFLYGSSLLYGLSGSTSLEAIGVALQTSTTPVAALSLVFVLATVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALALRILVGCFGAFDGQWKLLFTVLAVLSMTLGNVVALAQTSMKRMLAYSSIGQAGFVMIGMVCGTEDGFAAMVLYMAAYLFMNLGAFACIILFSIRTGSDRISDYAGLYQKDPLITLGLSLCLLSLGGIPPMLGFFGKIYLFFAGWADHQYLLVVVGLITSVVSIYYYISVIKMMVVKEPQEASDIVKAYPDVSWSVMGMQPLRVALIGCVAVTAVGGILSNPLFQWANTAVTSSPLLQEAIAQSTQRGLG

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Synechococcus sp. (strain CC9311)
Length
523 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.745 kDa
Sequence
MPELGSLLLSTQAVAAPGELLNLALHAGTVGPEAAVLVAMIATLLVDLAGEKVSVRWVPPICYAGLGSALVLLALQWNAPLEPSFLGAFLSDHLAIAFRAVVALSTLLSLLISWRYAEQSGTPVGEYAAILLAATLGGMLLCGATDLVSVFVSLETLSVASYLLSGYMKRDARSSEAALKYLLVGSAAAAVFLYGASLLYGLSGSTSLEVIGNALVTSPTPLAALALVFVLATVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALALRLLVGCFGSFDTQWKLLFTVLAILSMTLGNVVALAQTSMKRMLAYSSIGQAGFVMIGLVCGTEDGFAAMVLYMATYLFMNLGAFACIILFSIRTGSDRISDYAGLYQKDPLITLGLSLCLLSLGGIPPMLGFFGKIYLFFAGWADHQYVLVVVGLVTSVISIYYYIGVIKMMVVKEPQEASEVVKAYPPINWSTMGLPPLRVALVLCVLVTAVGGILSNPLFEWASSTVAGTPLLQQAIATSSGASLG

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Synechococcus sp. (strain CC9902)
Length
523 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.116 kDa
Sequence
MPEMGALLLATQAMAAPGELLNLSLNASAVLPEGAVLLAMIATLLVDLAGEKVAARWVPPICYIGLGSALVLLALQWNAPLEPSFLGAFLADNLAVAFRAVIATSTLLSLLISWRYAEKSGTPVGEYAAILLAATLGAMLLCGATDLVSIFISLETLSVASYLLSGYMKRDARSSEAALKYLLVGSAAAAVFLYGASLLYGLSGSTSLEVIGVALQTSTTPIAALSLVFVLATVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALALRILVGCFGAFDDQWKLLFTVLAVLSMTLGNVVALAQTSMKRMLAYSSIGQAGFVMIGMVCGTEDGFAAMVLYMAAYLFMNLGAFACIILFSIRTGSDRISDYAGLYQKDPLITLGLSLCLLSLGGIPPMLGFFGKIYLFFAGWANHEYLLVVVGLITSVISIYYYISVIKMMVVKEPHEASDVVKNYPDVDWSLMGMQPLRVALIGCVGVTAIGGILSNPLFQWANEAVAETPLLQQAIALVGERGLG

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Prochlorococcus marinus (strain MIT 9303)
Length
523 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.841 kDa
Sequence
MPEMGVFLLATQAMAAPGELLNLALNAGAIAPEGAVLVAMLATLLVDLAGEQAAARWVPPICYAGLGTALVLLAQQWNAPLEPSFLGAFLADNLAIAFRAVVALSTLLSLLISWRYAEQSGTPIGEYAAILLAATLGAMLLCGSTDLVSVFVSLETLSVASYLLAGYMKRDARSSEAALKYLLVGSAAAAVFLYGASLLYGLSGTTSLQAIGIALLTSPTPLAALSLVFVLATVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALALRLLVGCFGAFDNQWKLLFTVLAVLSMTLGNVVALAQTSMKRMLAYSSIGQAGFVMIGLVCGTEDGFAAMVLYMAAYLFMNLGAFACIILFSIRTGSDRISDYAGLYQKDPLITLGLSLCLLSLGGIPPMLGFFGKIYLFFAGWADHQYLLVVVGLVTSVVSIYYYISVIKMMVVKEPKEASDVVKSYPSIQWSTIGMPPLRIALVGCVVVTAVGGILSNPLFQWANNAVAGTPLLQEAIALGSQRSIG

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Prochlorococcus marinus (strain MIT 9313)
Length
523 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.837 kDa
Sequence
MPDMGVFLLATQAVAPPGELLNLALNAGAIAPEGAVLVAMLATLLVDLAGEQAAARWVPPICYAGLGTALVLLAQQWNAPLEPSFLGAFLADNLAISFRAVVALSTLLSLLISWRYAEQSGTPIGEYAAILLAATLGAMLLCGSTDLVSVFVSLETLSVASYLLAGYMKRDARSSEAALKYLLVGSAAAAVFLYGASLLYGLSGTTSLQAIGLALLTSPTPLAALSLVFVLATVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALALRLLVGCFGAFDNQWKLLFTVLAVLSMTLGNVVALAQTSMKRMLAYSSIGQAGFVMIGLVCGTEDGFAAMVLYMAAYLFMNLGAFACIILFSIRTGSDRISDYAGLYQKDPLITLGLSLCLLSLGGIPPMLGFFGKIYLFFAGWADHQYLLVVVGLVTSVVSIYYYISVIKMMVVKEPKEASDVVKSYPSIKWSTIGMPPLRIALVGCVVVTAVGGILSNPLFQWANNAVAGTPLLQEAIALGSQRSIG

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Acaryochloris marina (strain MBIC 11017)
Length
521 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.941 kDa
Sequence
MDVANLASQLNATTILPEGVLVISLILVLLGDITFGRSSAKWTPYLAIASLAACLYLLYTQWDQANPIGFLGSFNADNLSIVFRAIIALSTLVTILMSVRYIEQSGSSIGEFMTVLLTATVGAMFLCGAEELVMIFISLETLSIASYLMTGYMKRDSRSNEAALKYLLIGAASSAVFLYGLSLLYGLSGGKTHLDDIALALTDTSKSLALVISLVFVIASVSFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRLLTQAFPNLVEQWQFIFTALAILSMVLGNVVAIAQTSMKRMLAYSSIGQAGFVMIGLVIGTEAGYASMVFYLLIYLFMNLGAFTCVILFSLRTGTDEIGDYAGLYLKDPLLTLALSLCLLSLGGIPPLAGFFGKLYLFWAGWQAGAYGLVLLGLITSVVSIYYYIRVIKMMVVKEPQDMSEVIKNYPSIVWKPLGMRPLQVGLVLTLIATSLAGVLSNPLLTIVNSSVADVPRFKQATIPTSIDVAIQPDTPTIAPEL

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Synechococcus elongatus (strain PCC 7942)
Length
521 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.07 kDa
Sequence
MDFLTLAGQLNAGVILPEGIVIVTLLTVLVTDLILGRQSLRLTPALAITGLSAAIAVLTLQWNTSQNLAFLGGFNGDNLSIVFRGIVLLSAAVTILLSIRYVEQSGTSLGEFITILLTASLGGMFLSGANELVTIFVSLETLSISSYLLTGYMKRDPRSNEAALKYLLIGAASSAIFLYGVSLLYGLAGGETQLPAIAEKLGEAQPLALLISLIFVIAGIAFKISAVPFHQWTPDVYEGSPTPIVAFLSVGSKAAGFALAIRLLVTAYPALTEQWHFVFTALAILSLVLGNVVALAQTSMKRLLAYSSIAQAGFVMIGLIAGTEAGYSSMVYYLLIYLFMNLGGFACVILFSLRTGTDQISEYAGLYQKDPLVTLGLSLCLLSLGGIPPLAGFFGKLYLFWAGWQAGLYGLVLLALITSVISIYYYIRVIKMMVVKEPQEMSESVRNYPETNWNLPGMQPLRAGLVVCVIATAVAGILSNPLFNLASASVSGSSFLGLAPAAEVVTTTATPVALSEPPAAS

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Length
521 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.07 kDa
Sequence
MDFLTLAGQLNAGVILPEGIVIVTLLTVLVTDLILGRQSLRLTPALAITGLSAAIAVLTLQWNTSQNLAFLGGFNGDNLSIVFRGIVLLSAAVTILLSIRYVEQSGTSLGEFITILLTASLGGMFLSGANELVTIFVSLETLSISSYLLTGYMKRDPRSNEAALKYLLIGAASSAIFLYGVSLLYGLAGGETQLPAIAEKLGEAQPLALLISLIFVIAGIAFKISAVPFHQWTPDVYEGSPTPIVAFLSVGSKAAGFALAIRLLVTAYPALTEQWHFVFTALAILSLVLGNVVALAQTSMKRLLAYSSIAQAGFVMIGLIAGTEAGYSSMVYYLLIYLFMNLGGFACVILFSLRTGTDQISEYAGLYQKDPLVTLGLSLCLLSLGGIPPLAGFFGKLYLFWAGWQAGLYGLVLLALITSVISIYYYIRVIKMMVVKEPQEMSESVRNYPETNWNLPGMQPLRAGLVVCVIATAVAGILSNPLFNLASASVSGSSFLGLAPAAEVVTTTATPVALSEPPAAS

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
521 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.355 kDa
Sequence
MDFSSNVAAQLNAGTILPEGIVIVTLLLVLIVDLIGGRKVALALPYLAIAGLLVSVGLLVTSWSMADPIGFIGAFNGDNLSIIFRAIIALSTVVTILMSVRYVQQTGTSLAEFIAILLTATLGGMFLSAANELVMVFISLEMLSISSYLMTGYMKRDPRSNEAALKYLLIGASSSAIFLYGLSLLYGLSGGETQLVLIAEKLVNADTVGQSLGLAIALVFVIAGIAFKISAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFAVAIRLLVTAFGGITDEWHVIFTALAVLSMVLGNVVALAQTSMKRMLAYSSIGQAGFVMIGLVAGSEDGYASMVFYMLIYLFMNLGAFSCIILFTLRTGSDQISDYAGLYHKDPLLTLGLSICLLSLGGIPPLAGFFGKIYIFWAGWQSGLYGLVLLGLVTSVVSIYYYIRVVKMMVVKEPQEMSEVIKNYPAIKWNLPGMRPLQVGIVATLVATSLAGILANPLFNLATDSVVSTKMLQTALQQTGETPAIAISHDLP

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Cyanothece sp. (strain ATCC 51142)
Length
521 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.585 kDa
Sequence
MDFSSNIASQLNAGTILPEGIVIITLMVVLIGDLIGGRNARMWLPYGAIAGLLAALFALYTAWDNPSTIGFLGAFNGDNLSIVFRGIIALSTIVTLLMSIRYVEQTGTSLAEFIGIMLTATLGGMFLSGANELVMIFISLEMLSISSYLMTGYMKRDPRSNEAALKYLLIGASSSAIFLYGSSLLYGLSGGETTLDTISAKILASDGSSSLGLAIALVFVIAGIAFKISAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRLLVTAFSSIVDEWHLIFTALAILSMVLGNVVALAQTSMKRMLAYSSIGQAGFVMIGLTAGTDAGYSSMVFYLLVYLFMNLGAFSGVILFSLRTGTDQISEYAGLYQKDPLLTLGLSLCLLSLGGIPPLAGFFGKIYLFWAGWQAELYGLVLLALVTSVVSIYYYIRVVKMMVVKEPHEMSDSVKNYPEIRWNLEGMRPLQVGLVLSVIATSLAGILSNPLFSLANDSVTSTPILQSTIVNTRISQGEIPSSTIDP

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Length
520 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.443 kDa
Sequence
MDFANLAAQLNAGTILPEGIVIVTLMGVLIVDLILGRTSSRWIGYLAIAGLLAAIVALYFQWDATNPISFTGGFIGDDLSIIFRGIIALSAVVTILMSIRYVEQSGTALAEFIAILLTATLGGMFVSGASELVMIFISLETLSISSYLLTGYTKRDPRSNEAALKYLLIGASSTAVFLYGVSLLYGLSGGQTELSAIANGIITANVGQSLGAVIALVFVIAGIGFKISAAPFHQWTPDVYEGAPTPVIAFLSVGSKAAGFALAIRLLTTVFPFVAEEWKFVFTALAVLSMILGNVVALAQTSMKRMLAYSSIAQAGFVMIGLIAGTDAGYASMIFYLLVYLFMNLCGFTCIILFSLRTGTDQIAEYSGLYQKDPLLTLGLSISLLSLGGIPPLAGFFGKIYLFWAGWQAGLYWLVLLGLVTSVVSIYYYIRVVKMMVVKEPQEMSDVVKNYPEIRWNLPGFRPLQVGLVLTLIATSVAGILSNPLFTLANNSVANTAILQTTKVVSTQVSAIPAEKSEGL

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Length
520 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.465 kDa
Sequence
MDFANLAAQLNAGTILPEGIVIVTLMGVLIVDLILGRTSSRWIGYLAIAGLLAAIVALYFQWDATNPISFTGAFIGDDLSIIFRGIIALSAVVTILMSIRYVEQSGTALAEFIAILLTATLGGMFVSGASELVMIFISLETLSISSYLLTGYTKRDPRSNEAALKYLLIGASSTAVFLYGVSLLYGLSGGQTELNAIANGIITANVGQSLGAVIALVFVIAGIGFKISAAPFHQWTPDVYEGAPTPVIAFLSVGSKAAGFALAIRLLTTVFPFVAEEWKFVFTALAVLSMILGNVVALAQTSMKRMLAYSSIAQAGFVMIGLIAGTDAGYASMIFYLLVYLFMNLCGFTCIILFSLRTGTDQIAEYSGLYQKDPLLTLGLSISLLSLGGIPPLAGFFGKIYLFWAGWQAGLYWLVLLGLVTSVISIYYYIRVVKMMVVKEPQEMSDVVKNYPEIRWNLPGFRPLQVGLVLTLIATSVAGILSNPLFTLANNSVANTAILQATKVVSTQVSAIPAEKPDGL

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Prochlorococcus marinus (strain NATL2A)
Length
520 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.018 kDa
Sequence
MGELLSFQIFINEPVELLNLSLNAKAVLPEAAVLMAMLGTLLVDLAGEKISARWSPPICYAGLGSALILLAMQWDGEIQESFLGAFIADNLAIAFRGVIVLSTLISLLISWRYADQNGSPIGEFAAILLAATLGAMLLCGSTDLVSVFVSLETLSVASYLLSGYLKRDSRSSEAALKYLLVGSAAAAVFLYGASLLYGISGSTNLKEIGTTLLSAPTPLSALALVFVLSTVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRILVGCFSAFDTQWKLLFTVLAVLSMSLGNVVALAQKSMKRMLAYSSIGQAGFVMIGLVCGTEDGFAAMVLYMAAYLFMNLGAFACIILFSIRTGSDQISDYAGLYQKDPLITLGLSLCLLSLGGIPPMLGFFGKIYLFFAGWADGQYLLVTVGLVTSVISIYYYISVIKMMVVTEPKEASDVVKAYPSIEWSIPGMSSLKVALIFCVLVTAIGGIISNPLFNFADSAVNGTPLLREAITLASKSSIG

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Cyanothece sp. (strain PCC 8801)
Length
517 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.261 kDa
Sequence
MDFSSTIASQLNAGTILPEGIVIITLVGVLVGDLIFGRSSKSWLPYMAIIGLLASIVALYLAWDSPHPIGFLNSFNSDNLSIVFRAIIALSTAVTILMSIRYVEQTGTSLAEFIAIMLTATLGGMFLCGANELVMIFISLEMLSISSYLMTGYMKRDPRSNEAALKYLLIGASSSAIFLYGVSLLYGLSAGETALDAIATKIAAANGGESLGLAIALVFVIAGIAFKISAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRLLVTAFASVGEEWHFVFTALAILSMVLGNVVALAQTSMKRMLAYSSIGQAGFVMIGLVAGTDAGYSSMVFYLLVYLFMNLGAFACIILFSLRTGTDKISEYAGLYQKDPLLTLALSICLLSLGGIPPLAGFFGKIYLFWAGWQAELYGLVILGLVTSVVSIYYYIRVVKMMVVKEPQEMSDAVKNYPQIRWNLPGMRPLQVGIVLTLIATSLAGILSNPLFTLANDSVTSTPILQSAIINTRISQVPTESK

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Thermosynechococcus elongatus (strain BP-1)
Length
515 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.144 kDa
Sequence
MDLVTLAGQLNAGTILPETILIVTLLVVLLADLIQGRQADRWTPYFAIVGLGGAIATMIPLWTQPATISFFGSFISDHLSLFFRGLIALSALGTILMSIRYVEQTGSSLGEFMTILLTATVGGMFIAGAQELVFIFVALETLSIASYLLTGYTKRDSRSNEAALKYLLIGAASSAIFLYGSSLLYGLSGGHTQLPAIAQALSSESLGLVVALVFVIAGISFKISAVPFHQWTPDVYEGAPTPVVAFLSVGSKAAGFALAIRFLTLAFPSVTDQWQLIFTVLAILSMILGNVVALAQTSMKRMLAYSSIGQAGFVMIGFVVGTEAGYASMLFYLLVYLFMNLGAFTCVILFSLRTGTDQISEYAGLYQKDPLLTLGLSLCLLSLGGIPPLAGFFGKIYLFWAGWQAGAYGLVLLGLLTSVISIYYYIRVVKMMVVKEPQEMSEAVRNYPEVSWSSFGLRPLQVGLVMTVIATSLAGILANPLFNLVNTAVWDVPQLANQPTVMEVAYQALSPAGKS

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Cyanothece sp. (strain PCC 7424)
Length
514 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.14 kDa
Sequence
MDFSSFVASQLNAGTIWPEGIIIITLMVILIGDLIVGRSSKTWLPYVAIAGLLAAVVALYFEWDNPNTLSFLGAFNGDNLSIVFRAIVALSTTVTILMSVRYVEQSGTSLAEFIAIMLTATLGGMFLSGANELVMIFISLEMLSISSYLMTGYMKRDSRSNEAALKYLLIGASSSAIFLYGVSLLYGLSGGETTLDAIAAKITNVNGGQSLGLAIALVFVIAGIAFKISAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRLLVTAFALVSEQWHFIFTALAILSMVLGNVVALAQTSMKRMLAYSSIGQAGFVMIGLTANSDAGYSSMIFYLLIYLFMNLGAFICIILFALRTGTDQISEYSGLYQKDPLLTLGLSICLLSLGGIPPLAGFFGKIYLFWAGWQSGLYGLVLLGLVTSVISIYYYIRVVKMMVVKEPQDMSESVKNYPEIRWNLPGMRPLQVGLVLSVIATSLAGILSNPLFNLATDSVTSTPILQSAVISTQISQADK

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)
Length
513 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.857 kDa
Sequence
MNIDLAALNAGTLWPEYIVTITLIVVLLVDLISGRKASWSLPYLALLGLGIATATLLPMWILENPVSFLGSFTADPLSVVFRAFILISAALTVLMSVRYINQSSLATAEFYVLLLGATLGAMLLSGSSEMAMIFVALELLSITSYLLSGYAKLDKRSNEASLKYLLIGAASSGIFLYGMSLLYGFSGGQTQLTEIAPRIVNLGFPALLSLVLVAAGICFKLSAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRFMTSAYPGFSEQWQTLFVLLAILSMVLGNVVAIAQTSMKRMLAYSSIAQAGYVMIGLAIGTQEGYSSMILYIGTYLFMNLGAFMAVVLFSLRTGTDEITAYSGLYQKDPFLTLVLSLCLLSLAGIPPLAGFFGKLYLFWAAVQSQAYTLVFFGLVTSVASIYYYVRVVKLMLVKEPSPQVLAYSEAGDQDGIQTLKAGMLITTVATVVLGILFPPLISLADTSLRATPSLQQVRTATPVSRVSTGAQAPADHGR

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Microcystis aeruginosa (strain NIES-843)
Length
513 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.738 kDa
Sequence
MDFSSLVASQLNAGVIWPEGILIITLMVILIGDLIVGRSARSWLPYVAIAGLLAAVVALYFTWDNPKPVAFLGAFEGDNLSIVFRAIIALSTASTVLMSIRYVEQAGTSLAEFLAIMLTATLGGMFLSGASELVMIFISLEMLSISSYLMTGYMKRDPRSNEAALKYLLIGASSSAIFLYGVSLLYGLSGGETSLSAIAQKLTDVNGGQSLALAIALVFVIAGIAFKISAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGFALAIRLLVTVFGLVSEQWRFIFIALAILSMILGNVVALAQTSMKRMLAYSSIGQAGFVMIGLTAGTDAGYSSMIFYLLIYLFMNLGAFACVILFALRTGTDQIAEYSGLYQKDPLLTLCLSICLLSLGGIPPLAGFFGKIYLFWAGWQAGLYALVLVGLVTSVASIYYYIRVVKMMVVKEPQEMSDAVKNYPVINWTLTGMRPLQVGIVLSLVATSLAGILSNPLFTLATDSVTTTPILQSAALATHISRAN

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Staurastrum punctulatum
Length
513 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.091 kDa
Sequence
METNQLFSLDNLITILPECVLIICLLTILMIDVITKKSVWLSNIALLGLLTSTFILLFQLTNNEVGFTAFLGSFQVDGFTIAFRCLLTLSSALCIPLSTEYIRRSGMTQAEFLILLLTATLGGMFLCGANDLVTIFVSLECLSLSSYLLAGQAKKDIRSNEASLKYLLMGGASSSILVYGFSWLYGLSGGELQLSKIVNGISSQDIYLSSAVSLDGKTFGALGLWVAFVCILVGIGFKISAVPFHQWTPDVYEGSPTPVVAFLSVGSKAAGLALATRLLSIVFPAIEDQWHIVLEIVAFLSMVFGNLIAATQTSMKRMLAYSSISQAGYLLIAILVGNSDGYASMITYLLIYTFMNLGAFACTVIFGLRTGTDQIRDYTGLYLKDPWLAFALSICLLSLAGMPPLAGFFGKLYLFWCGWQSHLYLLVYTGLITSVISLYYYLRVVKAMMTKEVKEMSTYVREYVTPSMSIFSSSSIELGLTLCVLASSILGFFMNPLIDVTKQSMLVNNFLVF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, organellar chromatophore
Organism
Paulinella chromatophora
Length
512 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.053 kDa
Sequence
MENSGLLALPLNAATIVPEGAILLALLSSLLVDLAGEKTASRWVPPICYAGLGSALILLASQWNSTLSPSFLGAFLADNLAIAFRAIIATSTLFSLMISWRYVERSGAPMGEYAAILLAATLGAMFLCGSTDLVSIFVSLETLSVSSYLLAGYMKQDARSSEAALKYLLVGSATAAVFLYGASLLYGLTGGSTNLDAVALALQSSDTPVAALALVFVLATVAFKIAAVPFHQWTPDVYEGAPTPIVAFLSVGSKTAGFALALRLLVGCFESFDIQWKFLFSLLAILSMVLGNIVALSQTSMKRMLAYSSIGQAGFVMIGLVCGTEDGFAAMILYLATYLFMNMGAFACVILFSIRTGSDLIADYAGLYQKDPLVTIGLSLCLLSLGGIPPMLGFFGKIYLFFAGWADHQYLLVVTGLITSVVSIYYYISVIRMMVVIEPKEASDVVKSYAAVNWNIPGLNPLRVALLVCVIVTGIGGIFSNPLFQWANSAVAGTPILQKVIVTALGTTGTIS

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Chlorokybus atmophyticus
Length
511 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.376 kDa
Sequence
MEFKDLISSLNLIRLLPEGIVTILLVFILLIDLTFQKRVLSWLLYIPLVGLVCSMVVLLRQWGSQDTLSFLGSFQGDSLSIAFRFFILLSAVLCILLSKEYVERSRTALTEFFVLLLTAVIGGMLLSGANDLIMIFLSLETLGLSSYLLTGYMKKDLRSNEAAIKYLLIGAASSSILLYGLSLLYGLSGGAIEISTIAKNIVDKGLSQSFASWVALIFITVGIGFKVAAAPFHQWAPDVYEGSPTPVVAFLSVGSKAAGLALATRILTTLFPYLTNEWHLLFQVLASLSMILGNLIAISQTSMKRMLGYSSVSQAGFLMIGLIAGNPNGYSSMLVYMLLYIFMNLGAFACIILFGLKAGTDQIRDYAGLYRKDPFLVFCFSISLLSLGGIPPLAGFFGKLYLFWSGWQSGFYILVFIGLFTSVISIYYYLRVIKVMIVTEPQEMSIYVQRYTQRRWSITQLQPIELGIGLCVLGSVLAGVLVNPIINIAQQTVLYTPLLQQSEELMRTLTF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Allium textile
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.729 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFNGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVMSITALLFRWKEEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALISITVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNNGYASMITYMLFYISMNLGTFARIVSFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIEWSMTVCVIASTIPGISMNPILAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Trachelium caeruleum
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.736 kDa
Sequence
MIWHVQNDNFILNFTRIFMKAFHLPLFDGSFIFPECILIFGLILLLMIDSTSDQKDIPWLYFISSTSLVMSIMALLFRWREEPMISFSGNFQTNNFNEIFQVLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSFCSYLLSGYTKKDVRSNEATMKYLLMGGASSSILVHGFSWLYGLSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSPAPSHQWTPDVYEGSPTPVVAFLSVTSKVAASALATRIFDIPFYLSSNEWHLLLEILALLSMILGNLIAITQTSMKRMLAYSSIGQIGYIIIGIIVGDSNDGYASMITYMLFYISMNLGTFACIILFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLYLFWCGWQAGLYFLVLIALVTSVLSIYYYLKIIKLLMNGRNQEITPHVGNYRRSSLRSKNSIEFSMIVCVIASTIPGISMNPIIAIAQDSLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Yucca glauca
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.753 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVMSITALLFRWKEEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALISITVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFARIVSFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIEWSMTVCVIASTIPGISMNPILAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Ananas comosus
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.816 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVISITALLFRWREEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATMKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFACIVLFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLYLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPYVRNYRRSPLRSNNSIELSMTVCVIASTIPGISMNPILAIAQDXLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Asparagus officinalis
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.733 kDa
Sequence
MIWHVQNENFILDSTRILMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVMSITALLFRWKEEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALISTTVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFARIVSFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLYLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIEWSMTVCVIASTIPGISMNPILAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Brassica napus
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.616 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFDGSFIFPECILIFGLILLLMIDSTSDQKDIPWLYFISSTSFVMSITALLFRWREEPMISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKKDVRSNEATMKYLLMGGASSSTLVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSLAPSHQWTPDVYQGSPTPVVAFLSVTSKVAASALATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNGGYASMITYMLFYISMNLGTFACIILFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLHLFWCGWRAGLYFLVSIGLLTSVLSIYYYLKIIKLLMTGRNQEITPHVRNYRISPLRSTNSIELSMIVCVIASTIPGISMNPIIAIAQDSPF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Coelogyne cristata
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.695 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVMSITALFFRWREEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGLSWLYGLSGGEIELQEIVNGLINTQMYNSPGISIALISITVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSTEWHLLLEILAILSMILGNLIALTQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFACIVSFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLYLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIELSMTVCVIASTIPGISMNPILAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Ensete ventricosum
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.734 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLIISITALLFRWREEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATMKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALISITVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFACIVLFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPYVRNYRRSPLRSNNSIELSMTVCVIASTIPGISMNPILAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Leopoldia comosa
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.753 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVMSITALLFRWKEEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALISITVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFARIVSFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIEWSMTVCVIASTIPGISMNPILAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Maianthemum racemosum
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.741 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVMSITALLFRWKEEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALISTTVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFARIVSFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIEWSMTVCVIASTIPGISMNPILAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Muilla maritima
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.806 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVMSITALLFRWKEEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGLSGGEIELQEIVNGLINTQMYNSPGISIALISITVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFARIVSFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIEWSMTVCVIASTIPGISMNPILAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Narcissus elegans
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.748 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVMSITALLFRWKEEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDXITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALISITVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFARIVSFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLKSNNSIEWSMTVCVIAXTIPGISMNPILAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Phormium tenax
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.84 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDLTSDQKDRPWFYFISSTSLVMSITALLFRWKEEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDFITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALISITVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFARIVSFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIEWSMTVCVIASTIPGISMNPILAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Silene latifolia
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.699 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFDGSFIFPECILIFGLILLLIIDSTSDQKDIPWLYFISSTSLVMSITTLLFRWREEPMISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMALTEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKKDVRSNEATTKYLLMGGTSSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSPAPSHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFACIVLFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLYLFWCGWQAGLYLLVLIGLLTSVLSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSKNSIELSMIVCVIASTIPGISMNPIIAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Sisyrinchium montanum
Length
510 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.775 kDa
Sequence
MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVMSITALLFRWKEEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALISITVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFACIVSFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLYLFWCGWQAGLYFLVSMGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSTLRSNNSIEWSMTVCVIASTIPGISMNPILAIAQDTLF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Nephroselmis olivacea
Length
506 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.338 kDa
Sequence
MELSDILASFHASNLIPEGIVACTILLVLLLDLVYSRTCHAWLAWVAMAGLSLASVLLGQQWYQLMNLPTATMTFGGSFQADSLSLVFRAIIAMSCVLCILLSIDYVESTGTAPSEFLVLIATASLGGMLVAGSNDLLMMFVSLETLGLASYLLTGYMKRDVRSNEASLKYLLVGAASSGLFLYGISWMYGISGGHMELNSIAHAIVSLDETKTTTCALALVLMTVGVGFKVAAAPFHQWTPDVYQGSPTPVVAFLSVGSKAAGFILAVRMCTTLFPSFNTEWHLIFTILSILSMIVGNFIAVTQTSLKRMLGYSSVGQAGVMMIGMLTDSPDGYASLIVYLLIYLFMNLGAFACVILFGLRTGTDQIQDYSGLLARDPFLALCLSLCLLSLGGIPPLAGFFGKMYLFLAAWDAGQYSLVWVGLITSVVSIYYYLSVVKIMLVPATQEMSLAVREYPRRAWSLEPIQPLEVGIFVCVLGSILVGVAGNSMVNLMTITMSQAPSLGV

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Prochlorococcus marinus (strain MIT 9301)
Length
506 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.016 kDa
Sequence
MPNEIFTINLNAQAIIPEAFILLGIVGTLLVDLAGEKTASKWAPSICYLSIGSSLLSLTLQWNNPVESAFLGSFNSDNLAIAFRAIIALSTLVSLLISWRYTEQSGSPIGEFAAIVLSATLGAMLLCGSTDLISVFISLETLSVASYLLSGYLKRDPRSSEAALKYLLVGSAAAAVYLYGSSFLYGLSGSTNLTTIGLEIINKPSFITSLALVFVLSTVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKTAGFAFAIRILSTTFSSFDEEWKLLFTILAILSMALGNVVALAQTSMKRMLAYSSIGQAGFVMIGIVSGTQDGLSAAVLYLAAYLFMNLGAFSCVILFSLRTGSDRILDYSGLYQKDPLITLGLSLCLLSLGGLPPMLGFFGKIYLFFAGWANHQYLLVIVGLVTSVISIYYYISVIKMMVVKEPQEASEIVKSYPEVNWGIAGLPPLRVALYTCVAVTALGGILSNPLFKLANTAVSETPFLQDVIAAANNIS

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Prochlorococcus marinus (strain MIT 9215)
Length
506 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.073 kDa
Sequence
MPNEIFTINLNAQAIIPEAFILLGIVGTLLVDLAGEKTASKWAPIICYLSIGSSLLSLALQWSNPVESAFLGSFNSDNLAISFRAIISLSTLVSLLISWRYTEQSGSPIGEFAAIVLSATLGAMLLCGSTDLISVFISLETLSVASYLLSGYLKRDPRSSEAALKYLLVGSAAAAVYLYGSSFLYGLSGSTNLATIGLEIINKPSFITSLALVFVLSTVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKTAGFAFAIRILSTTFSSFDEEWKLLFTILAILSMALGNVVALAQTSMKRMLAYSSIGQAGFVMIGIVSGTQDGLSAAVLYLAAYLFMNLGAFSCVILFSLRTGSDRILDYSGLYQKDPLITLGLSLCLLSLGGLPPMLGFFGKIYLFFAGWANHQYLLVIVGLVTSVISIYYYISVIKMMVVKEPQEASEIVKSYPEINWGIVGLPPLRVALYTCVAVTALGGILSNPLFKLANTAVSETPFLQDIIATANNIS

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Prochlorococcus marinus (strain MIT 9515)
Length
506 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.28 kDa
Sequence
MPNEIFTINLNAQAIIPEAFILLGIVGTLLVDLAGEKTASRWAPVICYISLGSSLVSLAFQWSNPVNNAFLGSFNSDNLAIAFRSIIALSTLISLLISWRYTEQSGSPIGEFAAIVLSATLGAMLLCGSTDLVSVFISLETLSVASYLLSGYLKRDPRSSEAALKYLLVGSAAAAIYLYGSSFLYGLSGSTNLSTIGVEIINKPSFITSLSLVFVLSTVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKTAGFAFAIRILTTSFSSFDEQWKLLFTILAILSMALGNIVALAQTSMKRMLAYSSIGQAGFVMIGIVSGTQDGLSAAVLYLAAYLFMNLGAFSCVILFSLRTGSDRISDYSGLYQKDPLITLGLSLCLLSLGGLPPMLGFFGKIYLFFAGWANHQYLLVVVGLVTSVISIYYYISVIKMMVVKEPQEASEIVKSYPEIKWNIIGLPPLRIALYTCIAVTALGGILSNPLFKLANSAVSETPFLQDILAVTNNML

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Prochlorococcus marinus (strain MIT 9312)
Length
506 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.181 kDa
Sequence
MPNEIFTINLNAQAIIPEAFILLGIVGTLLVDLAGEKTASKWAPIICYLSIGSSLFSLALQWSNPVNSAFLGSFNSDNLAIAFRAIIALSTLVSLLISWRYTEQSGSPIGEFAAIVLSATLGAMLLCGSTDLISIFISLETLSVASYLLSGYLKRDPRSSEAALKYLLVGSAAAAVYLYGSSFLYGLSGSTNLATIGLEIINKPSFITSLALVFVLSTVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKTAGFAFAIRILSTTFSSFDEEWKLLFTILAILSMALGNVVALAQTSMKRMLAYSSIGQAGFVMIGIVSGTQDGLSATVLYLAAYLFMNLGAFSCVILFSLRTGSDRILDYSGLYQKDPLITLGLSLCLLSLGGLPPMLGFFGKIYLFFAGWANHQYLLVIIGLVTSVISIYYYISVIKMMVVKEPQEASEIVKSYPEINWGIVGMPPLRVALYTCVAVTALGGILSNPLFKLANTAVSETPFLQEIIAMANNIS

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4)
Length
506 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.22 kDa
Sequence
MPNEIFTINLNAQAIIPEAFILLGIVGTLLVDLAGEKTASRWAPVICYISLGSSLISLALQWSNPVNSAFLGSFNSDNLAIAFRSIIALSTLISLLISWRYTEQSGSPIGEFAAIVLSATLGAMLLCGSTDLVSVFISLETLSVASYCLSGYLKRDPRSSEAALKYLLVGSAAAAVYLYGSSFLYGLSGSTNLSTIGVEIINKPSFITSLSLVFVLSTVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKTAGFAFAIRILSTTFSSFDEQWKLLFTILAILSMALGNIVALAQTSMKRMLAYSSIGQAGFVMIGIVSGTQDGLSSAVLYLAAYLFMNLGAFSCVILFSLRTGSDRITDYSGLYQKDPLITLGLSLCLLSLGGLPPMLGFFGKIYLFFAGWANHQYLLVVVGLITSVISIYYYISVIKMMVVKEPQEASEIVKSYPEINWNIIGLPPLRIALYTCIAVTALGGILSNPLFKLANSAVSETPFLQNILAITNNVL

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2
Organism
Prochlorococcus marinus (strain AS9601)
Length
506 amino acids
Function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.141 kDa
Sequence
MPNEIFTINLNAQAIIPEAFILLGIVGTLLVDLAGEKTASKWAPIICYLSIGSSLVSLALQWSNPVENAFLGSFNSDNLAIAFRAIISLSTLISLLISWRYTEQSGSPIGEFAAIVLSATLGAMLLCGSTDLISVFISLETLSVASYLLSGYLKRDPRSSEAALKYLLVGSAAAAVYLYGSSFLYGLSGSTNLATIGLEIINKPSFITSLALVFVLSTVAFKIAAVPFHQWTPDVYEGSPTPVVAFLSVGSKTAGFAFAIRILSTTFSSFDEEWKLLFTILAILSMALGNVVALAQTSMKRMLAYSSIGQAGFVMIGIVSGTQDGLSAAVLYLAAYLFMNLGAFSCVILFSLRTGSDRILDYSGLYQKDPLITLGLSLCLLSLGGLPPMLGFFGKIYLFFAGWANHQYLLVIVGLVTSVISIYYYISVIKMMVVKEPQEASEIVKSYPEINWGIEGLPPLRIALYTCVAVTALGGILSNPLFKLANTAVSETPFLQDIIAIANNIS

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Huperzia lucidula
Length
505 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.702 kDa
Sequence
MNLDFDLYILYGNSILPECILILSLVILLIVDSIYGKKDTPWLYIIPFSGLVTSITVLFFQWEEEPIITFMGSFQINTFNKIFQFLILLCSVLCVPLSVDYIQCTEMAITEFLSFILTATLGATFLCGANDPVTIFVSLECLSLCSYLLSGYTKRDVRSNEATMKYLLMGGTSSSILAYGFSWLYGLSGGQTQLQEIAKGLISTQMYNSPGTSIAPICTMVGIGFKLSLVPFHQWTPDVYEGSPTPVVAFLSVVSKVAVSALAIRILNIVFPLSSNEWHSVLEILAISSMILGNFIAITQTSMKRMLAYSSISQIGYIMIGIIAGNSNGYTSVVTYMLFYIFMNLGTFACIILFSSRTGTDNIRDYAGLYLKDPLLASCFASCLLSLGGVPPLSGFFGKLYLFWCGWQAGLHSLVSIGLFTSVISIYYYLKIIKLLVTKRNEEVTPYITNYINSSYFLTSKNVTELSMMICVIASTVLGLAVNPIITMAQNSIFSSRFTSSLLIL

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Mesostigma viride
Length
502 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.973 kDa
Sequence
MEFKDLIASLNIDAVLPEAIIICSSLFILIIDLIFQRRANAVLPYMAILGLILSMLSLLFQWNGKEVTAFLGSFQTDSLSIAFRLLIALSSMLCVLLSIEYLENSKKTLSEFLVIFLTATLGAMLLCGSNDILMIFLSLETLGLCSYILTGYMKKDIRSNEASIKYLLIGAASSSILLYGFSLLYGLSHGHIEIHEIAANLIKDQNGNSLASLVALALIIVGISFKIAAAPFHQWAPDVYEGAPTPVVAFLSVSSKAAGLMLATRIMTILFPYIINEWHNIFQILAILSMAIGNIIAISQTNIKRMLGYSSIAQAGFLLVGLLAGNINGYSSMLVYMLIYLFMNLGAFACVILFSLKTGSDQIRDYGGLYLKDPILALCLSICLLSLGGIPPFGGFFGKLYLFWAGWEAGSYLLVFVGLLTSVISIFYYIKIIKMMIIKESPEVSFAIKNYSQKRWSIKDITPIEVSILICVIGTTISGIFVNPIISIAQQTVIDSSWLMAI

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Marchantia polymorpha
Length
501 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
56.19 kDa
Sequence
MKLELDMFFLYGSTILPECILIFSLLIILIIDLTFPKKDTIWLYFISLTSLLISIIILLFQYKTDPIISFLGSFQTDSFNRIFQSFIVFCSILCIPLSIEYIKCAKMAIPEFLIFILTATVGGMFLCGANDLVTIFVSLECLSLCSYLLCGYTKRDIRSNEAAIKYLLIGGTSSSILAYGFSWLYGLSGGETNIQKITNGLLNAETYNSSGTFIAFICILVGLAFKLSLVPFHQWTPDIYEGSPTPVVAFLSVTSKIAGLALATRILNILFSFSPNEWKIFLEILAILSMILGNLVAITQTSMKRMLAYSSISQIGYILIGLITGDLKGYTSMTIYVFFYIFMNLGTFACIILYSLRTGTDNIRDYAGLYIKDPLLSFSLTLCLLSLGGLPPLTGFFGKLYLFWCGWQSGFYLLVFIALITSVISLYYYLKIIKLILTKKNNEINPYIQAYIITSPTFFSKNPIEFVMIFCVLGSTFLGIIINPIFSFFQDSLSLSVFFIK

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Physcomitrella patens subsp. patens
Length
501 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.915 kDa
Sequence
MELELDLSFFYKTTILPECVLIFCLISILILDLILKIKDKNVFFFISLVSLLLSIFILIFQLKEEPVISFLGNFQADNFNKIFRIFIALCSILCIPLSIDFIKCTKLAITEFLIFLLTATIGGMFLCGANDLITIFVSLECLSLCSYLLSGYTKKDVRSNEAVMKYLLIGGTSSSILAYGFSWLYGLSGGEFQLQKIADGLVSTEMYNSFGSLLALVFIIVGIGFKLSLVPFHQWTPDVYEGSPTPVVAFLSVASKIAGLALLVRLFNIVFPFLPNQWHSLLEISAICSMILGNLVAITQTSMKRMLAYSSISQIGYLMIGLVTGNFDGYTSMIVYLLFYIFMNLGTFACIILFGLRTGTDNIRDYSGLILKDPLLTFSLALCLLSLGGIPPLSGFFGKLYLFWCAWKTGLYFLVFIGLFTSVISIYYYLKIIKLLITTENKEVTSYVQSYTVSSFSLLSKNSIEVSIIICVIASIFLGIFMNPIINILQINLHLNTFTNI

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Chaetosphaeridium globosum
Length
500 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.026 kDa
Sequence
MEIQNNLYGIDLYTILPESILIFCLLTTLIIDLSLDSKNKSWIIYLNTIGLILSGLFLCLQWNGIIPVTPFPSFKGDSFSIAFRFCIIIASLLSLLLSIDYIKRAGVQLMEFVIFLLGATIGGMFLCGANDLITIFTSLECLGLSSYLLAGYSKQDIRSNEAAMKYLLVGGASSAILAYGFSWLYGLSGGKIILSEIVDGLIFADFVNPLIKWITLTCIIVGLGFKISAVPFHQWTPDVYEGSPTPVVAFLSVASKTAGLALTIRIIATIFPYLENEWQFLLQILACLTMIVGNLVAITQTSMKRMLAYSSISQAGYLMIGIISSTNDGYASSLVYMLIYIFMNLGAFGCVILFGLRTGTDQIRDFSGLYLKDPWLASCLTIFLLSLGGIPPFAGFFGKIYLFWSGWQAGLYILTFVGLLTSVISIYYYLRIIKIMFVREAKEFSSYVKNYVIPVNSLLPQSSVETAMIVCMIASSVMGIAINPIIQVAQKTILSTIPFI

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Adiantum capillus-veneris
Length
498 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
54.81 kDa
Sequence
MNDINLFLAKLTYTSAKLTILPEIILILGLVAVVVIDLLSKGKNTFLLYKISMVTLLASAVILLWQWGFFTAYERSHARDFGNIFRFFLLICSLLSISSSVDYILCSKMSLAEFLLFKLAAGLGGMVLSCANDLVTIYVSLEFLALSSCFLSGYTKRDMRSNEATMKFLLMSGASSSLLLYGFSLLYGLSGGQLQLDKIVDGIIFNRYGSIIYLSAAFTTAGTAFKLSLFPFHQWTPDVYEGSPTPVVAFFSVTSKVAALALFTRLFGLIFPYFSNEWHVAVGLLATFSMILGNLIAVTQRSVKRMLAFSSISQIGYIMIGVLSADSGNGYASMITYTFIYILMNLGTFACITLFGLRTGTDNIRDYAGLYMKDPVLTFSLVLCLLSLGGMPPLSGFFGKLYLFWHGWKAGLYSLVLVALVTSVISIYYYLKIIKLMFTGKSGRSDTPLNSRQNSLVSLSISISKNSLEIAMIICALASTLSGIFIDPIIEITRNTFF

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Zygnema circumcarinatum
Length
497 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
53.902 kDa
Sequence
MPFDPLLFAQNTVILPEIIVIVCLLIVLVLDLIQENSAWLSTISLTGLVAATIALVFQWNHPSANDFLGSIQVDNFTISFRGIITISSALSILISTEYIKRAGMGLAECLIFILTATVGGLFLCGANNLVTVFVSLECLSLSSYLLVGYAKKDVRSNEASMKYLLMGGASSSIIAYGFSWLYGLSGGEIELSKLVDGITNHIDEPIAVWVALACVVVGIGFKLSAFPFHQWTPDVYEGSPTPVVAFFSVGSKAAALALATRMLSIVFPSIESEWHVLLELLALLSMIFGNLIAATQTSMKRMLAYSSISQAGYLIIGIVCGNIYGYTGMITYMVTYIFMNLGAFGCVILFGLRTGTDQIRDYTGLYLKDPLLAFCLSVCLLSLAGIPPLAGFFGKLYLFWCGWKSGLYLLVYVALITSVISMYYYLRVVKSMFTRETKEQSSYVRNYLAPSLSLLPTTSIEVGIALCVFISTTLGFVINPIISATSETLLATNTIVG

Gene
ndhB
Protein
NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
Organism
Chara vulgaris
Length
496 amino acids
Function
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I subunit 2 family.
Mass
55.628 kDa
Sequence
MYFQHQFSSLNLNSFLPEGILIFNIIFILILDLVSQKENKSMLVKISFIGLLLSMLTLIQQWYHESTIAFLGSFEVNHFTTCFRLIISLCCILCIPLSFEYIKCSGIRLTEFIIFLLFTTLGAMILSSANDLITIFISLECLGLGSYLLTGYVKKDIRSNEAGMKYLIIGGTSSSIFAYGLSWLYGLSGGSIYLKSIAYSFSHLNPSYSLASWFAYICIIVGIGFKLSLVPFHRWSPDVYEGSPTPVVAFLSIISKAGALALTIRISDIIFPILEQDSNSILQILAILSMIVGNLLAMVETSMKRILTYSSIAQAGYLLIGIVAGRNNGYASLLVYMIFYLFMNIGAFSCIILFGLRTGTDQIRDYTGLYTKDPWLASCLSLCLLSLAGIPPLTGFFGKILLFWSAWQSGFYFLVMTGIFTSIVSIYYYIRIVKFLVVAKEKDISYYVKKYSTYKSNSLMKQNPIELNIYLCTFISGFVGIFMNPVIYFAQQSILK