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nuoB1

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Roseiflexus sp. (strain RS-1)
Length
268 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
30.178 kDa
Sequence
MSDDREIQLEAEKHGVFLTTMQRFYNWGRRSSIWPLSFGLACCAIEMMATGLARFDLARFGAEMFRASPRQADLMIVAGTVTKKMAPQVVRLYNQMPEPRYVISMGACATSGGPFRDGYNVLRGIDLLIPVDVYIPGCPPRPEALLHALMTLQKQIDAQRLNQVRWYGKREAKEYPVPTFGKHGLEIDGKLIDPVGGLPLVSPYTSPTHGEMRSGMIEHPELVRHFPIMDETVERESPYKATGIAIEIAHNDLKRPAVEVDHAEDERR

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Length
264 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
29.108 kDa
Sequence
MAEIDPTQLELERQGILLTTVNRFYNWGRRSSIWPMAFGLACCAIEMMAFGLSRYDVARFGAELFRASPRQADLMIVAGTVTKKMAPQVVRLYNQMAEPRYVISMGACATSGGPFRDGYNVLRGIDLLIPVDVYVPGCPPRPEALLHALMTLQEQIDRQKLGRVRWYGSGDKPQTGDFPVPTFGAKGLEIDGKLVDPVGGLPLLSPYTSPSHGEHRSGQIEHPEVVRQFPIMDPEVELENALKARGIAPEIAADDLKRSVVNDA

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl)
Length
264 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
29.108 kDa
Sequence
MAEIDPTQLELERQGILLTTVNRFYNWGRRSSIWPMAFGLACCAIEMMAFGLSRYDVARFGAELFRASPRQADLMIVAGTVTKKMAPQVVRLYNQMAEPRYVISMGACATSGGPFRDGYNVLRGIDLLIPVDVYVPGCPPRPEALLHALMTLQEQIDRQKLGRVRWYGSGDKPQTGDFPVPTFGAKGLEIDGKLVDPVGGLPLLSPYTSPSHGEHRSGQIEHPEVVRQFPIMDPEVELENALKARGIAPEIAADDLKRSVVNDA

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71)
Length
221 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
24.683 kDa
Sequence
MRWSLSKPSDKPSGPATPGSSIIRDNGFEEDGRRSVLLTRLQDLVAWGRKNSVWPYNFGLSCCYVEMATSFTSKYDLARFGSEVIRASPRQADLIVISGTVFIKMAPVLQRLYDQMLEPRWVISMGSCANSGGMYDIYSVVQGVDRFLPVDVYVPGCPPRPDAFMQGLNLLQDAIGKEKRPLSWVIGPQGIERPAEESQRDLKRSGRMCATTLRSPDEVQK

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Koribacter versatilis (strain Ellin345)
Length
213 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
23.875 kDa
Sequence
MSNYAPADPRASSNRYRYNGTCMTNPSERFDNLVGSDQSFEQLRRATFGEQPEEGIVLTTLDNAVNWIRKNSIWPMTFGLACCAIEMMSMGASRFDIARFGAEVFRPSPRQSDLMIIAGRVSQKMAPVIRHLYLQMPEPKWVISMGACATSGGVFNNYALVQGVNQYIPVDIYVPGCPPRPEQLIYAITLLQEKIQAERGSFRRALNLEPVTP

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107)
Length
212 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
23.984 kDa
Sequence
MRWRLSKPQAATSIEQSKGSFEDAIRRNLLFAQLQDLVAWGRKNSLWPYNFGLSCCYVEMVTSFTSKYDIARFGAEVIRATPREADLMVISGTVFIKMAPVIKRLYEQMMEPRWVISMGSCANSGGMYDIYSVVQGVDKFLPVDVYVPGCPPRPDAFLEGLLLLQEAIGKEQRPLSWAIGPQGVERAPKPSLRDQRRAERQKATVFRSPDEV

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
Length
211 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
23.63 kDa
Sequence
MRWSLTRPGEEPGTPRDATMTETVKRNLVMGRLQDFVSWGQKNSIWPFNFGLSCCYVEMATAFTSKYDIARFGSEVLRATPREADLIVISGTVFVKMAPIVKYLYDQMLEPRWVISMGSCANSGGMYDIYSVVQGVDSFLPVDVYVPGCPPRPDALLEGLMLLQDSVGTQRRPLSWMVGPQGVERVTPPSLRDAKRDQRRAAQTLRSPDTI

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhodopseudomonas palustris (strain BisB5)
Length
208 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
23.205 kDa
Sequence
MTLPPAIPPTPADSMSVEEHMARSNLFTTLEDLTAWSRKHSLWPFNFGLSCCYVEQVTVLTPVYDQARFGAEVIRASPRQADLLVVSGTVFHKMAAPLLRLYEQMRAPRWVISMGACANSGGMYDIYSVVQGVDRFIPVDVYIPGCPPRPEAMLDALIMLQQQIGSERRPLGVTVGNTAGLGFDAPRRRDQRRDERMAQTLLDPPEKL

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhodopseudomonas palustris (strain BisA53)
Length
205 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
22.943 kDa
Sequence
MSYELQRPGEEMPIEEQMARTSLFTRLEDLVAWSRKNSLWPFNFGLSCCYVEQVTALTPVFDQARFGAEVIRASPRQADLLVVSGTVFHKMAAPLLRLYEQMRAPRWVISMGACANSGGMYDVYSVVQGVDSFLPVDVYIPGCPPRPEAVLDALILLQQQVGAQRRPLGVTVGNAAGLGFEAPRRRDQRRDERMAQTLLDPPEKL

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Length
205 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
22.879 kDa
Sequence
MSWTIGRPGAEAPEDRMAASHLFTRLDDLVAWSRKHSLWPFNFGLSCCYVEMATALTPVYDQARFGAEVIRSTPRQADLLIVSGTVFRKMAVPLYRLYQQMREPRWVISMGACANSGGMYDIYSVVQGVDSFLPVDVYVPGCPPRPEALMEALVLLQSKIATEARPLQIRMGETGPARPFDPVPRRDALREGRMSVARLADPEST

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhodopseudomonas palustris (strain BisB18)
Length
201 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
22.022 kDa
Sequence
MGLSPNATTAGPRLPRPLVAPAATGILDPRTGRPVGADDRFFLEVNNELADKGFFVAATDDLITWARTGSLMWMTFGLACCAVEMMQMSMPRYDAERFGFAPRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYAVVRGCDRIVPIDIYVPGCPPTAEALLYGVMLLQKKIRRTGTIER

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
Length
199 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
21.846 kDa
Sequence
MIHVVDTVTEPVEIEQGIKIVPAANTIITTLDKIASWGRCSSLWPLTFGLACCAIEMMATAASHYDLDRFGIIMRATPRQADVMIIAGTVTKKMAPVIVNLYHQMPEPRYVIAMGSCACSGGIFNTYSTVQGVDEILPVDVYIPGCPPRPEALIEGLLKLQEKIKTEPHKKTGCLSGVCLIDKSQRRCSYESCRDNKKD

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Length
198 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
21.799 kDa
Sequence
MQPTPSQHPVGAQPLIARPATGIIDPNTGRPVGADDPFFLNVNRELSDKGFFVAATDDLITWARTGSLMWMTFGLACCAVEMMQLSMPRYDAERFGFAPRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRIVPIDIYVPGCPPTAEALLYGVMLLQKKIRRTGTIER

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhodopseudomonas palustris (strain TIE-1)
Length
198 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
21.799 kDa
Sequence
MQPTPSQHPVGAQPLIARPATGIIDPNTGRPVGADDPFFLNVNRELSDKGFFVAATDDLITWARTGSLMWMTFGLACCAVEMMQLSMPRYDAERFGFAPRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRIVPIDIYVPGCPPTAEALLYGVMLLQKKIRRTGTIER

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhizobium etli (strain CIAT 652)
Length
194 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
21.295 kDa
Sequence
MGVTPVSNEPLVAQQPKGIIDPSTGKPIGSNDAFFGEINNELADKGFLVTSTDELINWARTGSLMWMTFGLACCAVEMMQLSMPRYDVERFGFAPRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRVVPIDIYVPGCPPTAEALLYGVLLLQKKIRRTGTIER

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhizobium etli (strain CFN 42 / ATCC 51251)
Length
194 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
21.294 kDa
Sequence
MGVTPVSNQPLVAQQPKGIIDPSTGKPIGSNDAFFGEINNELADKGFLVTSTDELINWARTGSLMWMTFGLACCAVEMMQLSMPRYDVERFGFAPRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRVVPIDIYVPGCPPTAEALLYGVLLLQKKIRRTGTIER

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Sorangium cellulosum (strain So ce56)
Length
194 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
21.481 kDa
Sequence
MGEVKAGGPSTRVMEGSEHGFATTRVDALLNWAKKYSLFQYPFVTACCGMEYMAMASPRFDMARFGAEVPRFSPRQADLLWVVGTISQRQAPALKRIYEQMADPKWVLAFGTCASCGGFYDNYTTVAGIDKVIPCDVYVPGCPPRPEAVLDGLMLLQDKIARGDRTPAIVKPREDPAQTTEHLVTLQRKERSLP

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhizobium meliloti (strain 1021)
Length
192 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
21.002 kDa
Sequence
MELASGTTLVAPQPKGILDPATGKPIGSNDAFFGEINNELADKGFLVTSTDELINWARTGSLMWMTFGLACCAVEMMQMSMPRYDAERFGFAPRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRVVPVDIYVPGCPPTAEALLYGVLLLQKKIRRTGTIER

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Salinispora arenicola (strain CNS-205)
Length
188 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
20.169 kDa
Sequence
MQVPAVLGEPIRFVLNWGRRYSLWVFNFGLACCAIEFIATSMSRHDFMRLGVIPFAHGPRQADLMVVSGTVTDKMAPAIKRLYDQMPEPKYVISFGACSNCGGPYWDSYSVTKGVDQLIPVDVYVPGCPPRPEALLHGILRLQEKIAAEGAGVGGVSRPDALASPTGGAAPRSADSLTAPLVRPPTPS

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
Length
188 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
20.334 kDa
Sequence
MQVPAVLGEPIRFVLNWGRRYSLWVFNFGLACCAIEFIATSMSRHDFMRLGVIPFAHGPRQADLMVVSGTVTDKMAPAIKRLYDQMPEPKYVISFGACSNCGGPYWDSYSVTKGVDQLIPVDVYVPGCPPRPEALLHGILRLQEKIAAEEAGVGGVSRPDALASPADALPPRAADSLTAPPVRPPDPS

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Solibacter usitatus (strain Ellin6076)
Length
188 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
21.21 kDa
Sequence
MSSFIQNQFEQNFITTNVDHVFNWARKSALWPLTFGLACCAIEMIASSTSRFDIARFGAEVFRPSPRQSDLMIVAGTVTLKMAPVLKRIWDQMPDPKWCISMGACSSVGGPFNTYAVLQGVDKIVPVDVYVTGCPPRPENLFYALLKLQDKIDTMTTLVKRPTEVRLDETMLEEFKQQIRIAQIQNPA

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Acidiphilium cryptum (strain JF-5)
Length
186 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
20.745 kDa
Sequence
MNAVQQPDIAWNRDHLDPGAEQEAVIRGITGEIAGKGFVVANLDRLVNWARTGSLWPMTFGLACCAVEMIHAYMPRWDLDRFGIIPRNSPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALVYGITQLQKKIRRTGTIFRE

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Chloroherpeton thalassium (strain ATCC 35110 / GB-78)
Length
186 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
20.636 kDa
Sequence
MSGQQGMGDGFLTTTLDAITNWGRANSIWPMPMGLSCCAIEMMAMAGPRYDIARFGAEVFRFSPRQSDLMIVAGTVTYKMATVVKKIWDQMPEPKWCIAMGACSSSGGMFRSYPVVQGIDQFLPVDVYVPGCPPRPDAVIHAVMEIQEKIKRQKDSFQDSFLAEDDAPQVRQPESPKEKEKLTVSE

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Length
184 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
19.996 kDa
Sequence
MGLEEKLPSGFLLTTVEQAAGWVRKASVFPATFGLACCAIEMMTTGAGRYDLARFGMEVFRGSPRQADLMIVAGRVSQKMAPVLRQVYDQMPNPKWVISMGVCASSGGMFNNYAIVQGVDHIVPVDIYLPGCPPRPEMLIDAILKLHQKIQSSKLGVNAEEAAREAEEAALKALPTIEMKGLLR

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
184 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
20.017 kDa
Sequence
MGLEEKLPSGFLLTTVEQAAGWVRKSSVFPATFGLACCAIEMMTTGAGRYDLARFGMEVFRGSPRQADLMIVAGRVSQKMAPVLRQVYDQMPNPKWVISMGVCASSGGMFNNYAIVQGVDHVVPVDIYLPGCPPRPEMLMDAILKLHQKIQSSKLGVNAEEAAREAEEAALKALPTIEMKGLLR

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Length
184 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
20.025 kDa
Sequence
MGLEEKLPSGFVLTTVEQAAGWVRKSSVFPATFGLACCAIEMMTTGAGRYDLARFGMEVFRGSPRQADLMIVAGRVSQKMAPVLRQVYDQMPNPKWVISMGVCASSGGMFNNYAIVQGVDHIVPVDIYLPGCPPRPEMLLDAILKLHQKIQTSKLGVNAEEAAREAEEAALKALPLIEMKGLLR

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Anaeromyxobacter dehalogenans (strain 2CP-C)
Length
182 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
20.128 kDa
Sequence
MASELDGLPVIATRREEAEGFLQGLVSKSLGWARKYSLFTYPFVTACCGMEYMTMASARYDSDRFGAAMPRFSPRQADLLMVVGTVNCKQAPILQRIYEQMADPKWVMAFGVCASSGGFYDNYATVQGIDRIIPVDVYVPGCPPRPEQVLDGIMLLQKKIQNQSHKLIDRKPLPVIAGGPGR

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95)
Length
179 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
19.604 kDa
Sequence
MGLEEKAGDLGIVTTTLEGVVNWGRTKAMWPMLFGLACCAIEMMAGQASNYDMSRFGLELMRASPRQADLMIVAGRVSRKMAPVLRRLYDQMPEPKWVVAMGDCASCGGVYNNYAIVQGVDEIVPVDVYVAGCPPRPEALIDGILQLHEKIKRDKITDHADGKPIRIEQAERGALKPLG

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
Length
178 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
19.949 kDa
Sequence
MSLLDHKFGQGGIVVSQLEDVLNWARLSSLFPMSFGLACCAIEMMQTFTSGYDLDRFGVIPRPSPRQSDVMIVAGTVTFKMADRIRRLYEQMPEPRYVISMGSCSNCGGPYWEHGYHVVKGVDRIVPVDIYVPGCPPRPEALIGGFLKLQEKIRKETLVAPKAVERFLETHAKEKNIA

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)
Length
176 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
19.641 kDa
Sequence
MAMTGLNTAGSDRDYDTQSLNRELQDKGFLLTTTEDLINWARTGSLHWMTFGLACCAVEMMHTSMPRYDVERFGVAPRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGILQLQRKIRRTGTITR

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Length
176 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
19.641 kDa
Sequence
MAMTGLNTAGSDRDYDTQSLNRELQDKGFLLTTTEDLINWARTGSLHWMTFGLACCAVEMMHTSMPRYDVERFGVAPRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGILQLQRKIRRTGTITR

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Chloroflexus aggregans (strain MD-66 / DSM 9485)
Length
174 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
19.123 kDa
Sequence
MGIEEKAGNLGIVTTTLETVVNWGRTNAMWPLLFGLACCAIEMMGAQASNYDLSRFGMELNRASPRQADLMIVAGRVSRKMAPVVRRLYDQMPEPKWVIAMGDCAACGGIFNNYAIVQGVDEVVPVDVYVAGCPPRPEALIDGIMMLHQKVMREKLSGKKEAPIRIDQPLVQVK

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Rhodobacter sphaeroides (strain KD131 / KCTC 12085)
Length
174 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
19.438 kDa
Sequence
MTGLNTAGSDRDYDTQSLNRELQDKGFLLTTTEDLINWARTGSLHWMTFGLACCAVEMMHTSMPRYDVERFGVAPRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGILQLQRKIRRTGTITR

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Anaeromyxobacter sp. (strain K)
Length
173 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
18.758 kDa
Sequence
MAARMDPGIGGDVTLLHTSQLDNLINLARASSLYYLTFGLACCGIELMQTGGPRADVMRFGAIPRASPRQADFMIVAGTLTYKMAERARLLYDQMPEPKYVISMGSCSNCGGLFQLGYSVCKGVDKVIPVDVYVPGCPPRPEALTEGLLRLQEIVRSEPWSTKRRPAAQAEGA

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Anaeromyxobacter sp. (strain Fw109-5)
Length
172 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
18.883 kDa
Sequence
MTARTMDAGTGDVTLFHTSQLDKLINMARENSLWYLLFGLACCGIELMQFGGPRADVMRFGAIPRASPRQADFMIVAGTLTYKMAERAKLLYDQMPEPKYVISMGSCSNCGGLFQLGYSVCKGVDKVIPVDVYVPGCPPRPEALTEGLIRLQELIRSEPWATKRRPAKGSAA

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1)
Length
171 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
18.796 kDa
Sequence
MVSSNTDLTYSSAIEGGIVVSKADAVINWIRTNSMWPMPMGLACCAIELMQVGNGRFDIARFGAEVMRFSPRQSDCMIVAGSVTYKMAPQIRRIYDQMMSPKWVIAMGACASSGGMYRSYAHMQGVDRILPVDVYISGCPPRPEGILDALMKLQAKIRTERAGQNLFKATV

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Roseiflexus castenholzii (strain DSM 13941 / HLO8)
Length
167 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
18.33 kDa
Sequence
MGIEQKAGDMGIVTASLEQVVNWSRSNAMWPLLFGLACCAIEMMGAQGANYDLSRFGMEINRASPRQADLMIVAGRVSRKMAPVVRRLYDQMADPKWVIAMGDCAACGGVFNNYAIVQGVDEIVPVDVYVAGCPPRPEALIDGIIHLHEKVRRMRLDGTLREPVHLS

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Symbiobacterium thermophilum (strain T / IAM 14863)
Length
166 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
18.213 kDa
Sequence
MSADGVFRDQGGFVTTTVDSFLRWAQSNSIWPLTFGLACCAIEMMNLASGPRYDIARFGSEAFRASPRQADLIFISGRVSNKMAPVIKRVYSQMLEPKWVVAFGACASSGGIFDNYAIMQGVDNLLPVDIYVPGCPPTPEAVIYAVQKLRDRIRKEDPRGGIIVRG

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B
Organism
Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1)
Length
163 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
18.476 kDa
Sequence
MAMMEYLTTRKDELIGWVRKFSIFPYPFVTACCGMEFMAVASTLYDTDRFGAALPRFTPRQSDLLMVVGTITHKEAPVIKRVYDQMCDPKWVMAFGACATSGGVYRNYTVLQGVDRIIPVDIYIPGCPPRPEMVIDAIMKLQDKIAGERHPIFPYEKQNPVPV

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Burkholderia mallei (strain NCTC 10247)
Length
159 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
17.533 kDa
Sequence
MSIEGVLKEGFVTTTADKLINWTRTGSLWPMTFGLACCAVEMMHAGAARYDLDRFGVVFRPSPRQSDVMIVAGTLCNKMAPALRRVYDQMAEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGVIQLQAKIRRTSTIARQ

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Burkholderia mallei (strain NCTC 10229)
Length
159 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
17.533 kDa
Sequence
MSIEGVLKEGFVTTTADKLINWTRTGSLWPMTFGLACCAVEMMHAGAARYDLDRFGVVFRPSPRQSDVMIVAGTLCNKMAPALRRVYDQMAEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGVIQLQAKIRRTSTIARQ

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Burkholderia mallei (strain ATCC 23344)
Length
159 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
17.533 kDa
Sequence
MSIEGVLKEGFVTTTADKLINWTRTGSLWPMTFGLACCAVEMMHAGAARYDLDRFGVVFRPSPRQSDVMIVAGTLCNKMAPALRRVYDQMAEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGVIQLQAKIRRTSTIARQ

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Burkholderia mallei (strain SAVP1)
Length
159 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
17.533 kDa
Sequence
MSIEGVLKEGFVTTTADKLINWTRTGSLWPMTFGLACCAVEMMHAGAARYDLDRFGVVFRPSPRQSDVMIVAGTLCNKMAPALRRVYDQMAEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGVIQLQAKIRRTSTIARQ

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Burkholderia pseudomallei (strain 1106a)
Length
159 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
17.533 kDa
Sequence
MSIEGVLKEGFVTTTADKLINWTRTGSLWPMTFGLACCAVEMMHAGAARYDLDRFGVVFRPSPRQSDVMIVAGTLCNKMAPALRRVYDQMAEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGVIQLQAKIRRTSTIARQ

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Burkholderia pseudomallei (strain 1710b)
Length
159 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
17.533 kDa
Sequence
MSIEGVLKEGFVTTTADKLINWTRTGSLWPMTFGLACCAVEMMHAGAARYDLDRFGVVFRPSPRQSDVMIVAGTLCNKMAPALRRVYDQMAEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGVIQLQAKIRRTSTIARQ

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Burkholderia pseudomallei (strain 668)
Length
159 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
17.533 kDa
Sequence
MSIEGVLKEGFVTTTADKLINWTRTGSLWPMTFGLACCAVEMMHAGAARYDLDRFGVVFRPSPRQSDVMIVAGTLCNKMAPALRRVYDQMAEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGVIQLQAKIRRTSTIARQ

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Burkholderia pseudomallei (strain K96243)
Length
159 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
17.533 kDa
Sequence
MSIEGVLKEGFVTTTADKLINWTRTGSLWPMTFGLACCAVEMMHAGAARYDLDRFGVVFRPSPRQSDVMIVAGTLCNKMAPALRRVYDQMAEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALVYGVIQLQAKIRRTSTIARQ

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Acidithiobacillus ferrooxidans (strain ATCC 53993)
Length
158 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
17.48 kDa
Sequence
MGIEGILEKGFVTTSIDTVVNWSRTGSLWPMTFGLACCAVEMMHAGAARYDLDRFGLLFRPSPRQSDLMIVAGTLVNKMAPALRKVYDQMPEPRWVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALIFGLIQLQKKIRRTNTIAR

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Azoarcus sp. (strain BH72)
Length
158 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
17.51 kDa
Sequence
MSIEGVFREGFVTTSLDAVINWTRTGSLWPMTFGLACCAVEMIHAGCSRYDLDRFGVVFRPSPRQSDLMIVAGTLCNKMAPALRKVYDQMAEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALLYGIIQLQNKIKRTNTIAR

Gene
nuoB1
Protein
NADH-quinone oxidoreductase subunit B 1
Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Length
158 amino acids
Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Similarity
Belongs to the complex I 20 kDa subunit family.
Mass
17.408 kDa
Sequence
MGVEGILEKGFVTTTADKLINYTRTGSLWPMTFGLACCAVEMMHAGAARYDLDRFGVVFRPSPRQSDLMIVAGTLCNKMAPALRKVYDQMAEPRWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALLYGIIQLQNKIKRTNTIAR