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nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoD nuoD nuoC nuoC nuoB nuoB nuoA nuoA ndh ndh qor qor lpdC lpdC ndhA ndhA hycE hycE Rv0083 Rv0083 nuoJ nuoJ nuoK nuoK nuoL nuoL nuoM nuoM nuoN nuoN lpdA lpdA
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
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nuoIProbable NADH dehydrogenase I (chain I) NuoI (NADH-ubiquinone oxidoreductase chain I); 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 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. (211 aa)
nuoHProbable NADH dehydrogenase I (chain H) NuoH (NADH-ubiquinone oxidoreductase chain H); 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 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. (410 aa)
nuoGProbable NADH dehydrogenase I (chain G) NuoG (NADH-ubiquinone oxidoreductase chain G); 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 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 (By similarity). (806 aa)
nuoFProbable NADH dehydrogenase I (chain F) NuoF (NADH-ubiquinone oxidoreductase chain F); 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 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 (By similarity); Belongs to the complex I 51 kDa subunit family. (445 aa)
nuoDProbable NADH dehydrogenase I (chain D) NuoD (NADH-ubiquinone oxidoreductase chain D); 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; Belongs to the complex I 49 kDa subunit family. (440 aa)
nuoCProbable NADH dehydrogenase I (chain C) NuoC (NADH-ubiquinone oxidoreductase chain C); 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; Belongs to the complex I 30 kDa subunit family. (236 aa)
nuoBProbable NADH dehydrogenase I (chain B) NuoB (NADH-ubiquinone oxidoreductase chain B); 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. (184 aa)
nuoAProbable NADH dehydrogenase I (chain A) NuoA (NADH-ubiquinone oxidoreductase chain A); 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; Belongs to the complex I subunit 3 family. (128 aa)
ndhRv1854c, (MTCY359.19), len: 463 aa. Probable ndh,NADH dehydrogenase (see citations below), similar to several e.g. S74826 NADH dehydrogenase from Synechocystis sp. (445 aa), FASTA score: opt: 1228, E(): 0, (46.3% identity in 432 aa overlap). Highly similar to Rv0392c|Z84725|g1817703 from Mycobacterium tuberculosis (470 aa), FASTA scores: opt: 1911, E(): 0, (64.7% identity in 459 aa overlap); and Rv1812c. (463 aa)
qorProbable quinone reductase Qor (NADPH:quinone reductase) (zeta-crystallin homolog protein); Rv1454c, (MTV007.01c), len: 328 aa. Probable qor,quinone oxidoreductase, simiar to U87282|RCU87282_2 quinone oxidoreductase from Rhodobacter capsulatus (323 aa), FASTA scores: opt: 849, E(): 0, (44.7% identity in 329 aa overlap). Also similar to MTCY180.06 Hypothetical protein from Mycobacterium tuberculosis (334 aa), FASTA scores: opt: 430, E(): 2e-14, (32.3% identity in 350 aa overlap). Contains PS01162 Quinone oxidoreductase / zeta-crystallin signature. (328 aa)
lpdCDihydrolipoyl dehydrogenase; Lipoamide dehydrogenase is an essential component of the alpha-ketoacid dehydrogenase complexes, namely the pyruvate dehydrogenase (PDH) complex, the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, and likely also the 2-oxoglutarate dehydrogenase (ODH) complex. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes. Is also able to catalyze the transhydrogenation of NADH and thio-NAD(+) in the absence of D,L- lipoamide, and the NADH-dependent reduction of [...] (464 aa)
ndhARv0392c, (MTCY04D9.04c), len: 470 aa. Probable ndhA,membrane NADH dehydrogenase, equivalent to many e.g. AF038423|AF038423_1 NADH dehydrogenase from Mycobacterium smegmatis (457 aa), FASTA scores: opt: 1991, E(): 0, (67.9% identity in 458 aa overlap); MLCB1788_3 NADH dehydrogenase from Mycobacterium leprae (466 aa), FASTA score: (62.5% identity in 467 aa overlap). Also similar to others from several organisms e.g. P00393|DHNA_ECOLI|66211|581140|CAA23586.1|V00306 NADH dehydrogenase from Escherichia coli (434 aa); and Rv0392c|ndhB from Mycobacterium tuberculosis. Has hydrophobic stretch [...] (470 aa)
hycEPossible formate hydrogenase HycE (FHL); Rv0087, (MTCY251.05), len: 492 aa. Possible hycE (alternate gene name: hevE), formate hydrogenlyase, similar to others. Belongs to the complex I 49 kDa subunit family. (492 aa)
Rv0083Probable oxidoreductase; Rv0083, (MTV030.27, MTCY251.01), len: 640 aa. Probable oxidoreductase, showing some similarity to other various oxidoreductases. Nucleotide position 91071 in the genome sequence has been corrected, T:C resulting in I224I. (640 aa)
nuoJProbable NADH dehydrogenase I (chain J) NuoJ (NADH-ubiquinone oxidoreductase chain J); 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. (262 aa)
nuoKProbable NADH dehydrogenase I (chain K) NuoK (NADH-ubiquinone oxidoreductase chain K); 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; Belongs to the complex I subunit 4L family. (99 aa)
nuoLProbable NADH dehydrogenase I (chain L) NuoL (NADH-ubiquinone oxidoreductase chain L); 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 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 (By similarity). (633 aa)
nuoMProbable NADH dehydrogenase I (chain M) NUOK (NADH-ubiquinone oxidoreductase chain M); 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 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 (By similarity). (553 aa)
nuoNProbable NADH dehydrogenase I (chain N) NuoN (NADH-ubiquinone oxidoreductase chain N); 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; Belongs to the complex I subunit 2 family. (531 aa)
lpdANAD(P)H quinone reductase LpdA; May contribute to virulence by increasing resistance to reactive oxygen intermediates. It can reduce 2,6-dimethyl-1,4- benzoquinone (DMBQ), 5-hydroxy-1,4-naphthaquinone (5-HNQ) and menadione. NADPH is the physiological reductant rather than NADH. (493 aa)
Your Current Organism:
Mycobacterium tuberculosis H37Rv
NCBI taxonomy Id: 83332
Other names: M. tuberculosis H37Rv, Mycobacterium sp. H37Rv, Mycobacterium tuberculosis str. H37Rv, Mycobacterium tuberculosis strain H37Rv
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