STRINGSTRING
AHM62513.1 AHM62513.1 AHM58335.1 AHM58335.1 AHM58725.1 AHM58725.1 AHM59059.1 AHM59059.1 AHM59283.1 AHM59283.1 AHM59591.1 AHM59591.1 AHM59598.1 AHM59598.1 nuoB nuoB AHM60142.1 AHM60142.1 AHM60534.1 AHM60534.1 AHM60579.1 AHM60579.1 AHM60859.1 AHM60859.1 AHM61214.1 AHM61214.1 AHM61230.1 AHM61230.1 AHM61798.1 AHM61798.1 AHM62184.1 AHM62184.1 nuoK nuoK AHM62188.1 AHM62188.1 AHM62419.1 AHM62419.1 AHM62420.1 AHM62420.1 AHM62421.1 AHM62421.1 AHM62471.1 AHM62471.1 AHM62473.1 AHM62473.1 AHM62485.1 AHM62485.1 AHM62702.1 AHM62702.1 AHM62705.1 AHM62705.1 AHM62708.1 AHM62708.1 AHM62815.1 AHM62815.1 AHM62946.1 AHM62946.1 AHM63030.1 AHM63030.1 AHM63059.1 AHM63059.1 AHM63437.1 AHM63437.1 AHM63457.1 AHM63457.1 AHM63459.1 AHM63459.1 AHM63630.1 AHM63630.1 AHM63633.1 AHM63633.1 AHM63634.1 AHM63634.1 AHM63636.1 AHM63636.1 AHM63637.1 AHM63637.1 AHM63640.1 AHM63640.1 AHM63641.1 AHM63641.1
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
AHM62513.1Hypothetical protein; COG1145 Ferredoxin. (115 aa)
AHM58335.1COG1428 Deoxynucleoside kinases. (220 aa)
AHM58725.1Cytochrome c class I; COG2133 Glucose/sorbosone dehydrogenases. (680 aa)
AHM59059.1PKD domain-containing protein; COG3828 Uncharacterized protein conserved in bacteria. (259 aa)
AHM59283.1Hypothetical protein. (170 aa)
AHM59591.12-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase; COG0801 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase. (160 aa)
AHM59598.1COG0479 Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit. (250 aa)
nuoBNADH:ubiquinone oxidoreductase; 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. (176 aa)
AHM60142.1Hypothetical protein; COG2010 Cytochrome c, mono- and diheme variants. (111 aa)
AHM60534.1COG2010 Cytochrome c, mono- and diheme variants. (234 aa)
AHM60579.1COG3828 Uncharacterized protein conserved in bacteria. (1148 aa)
AHM60859.1COG2010 Cytochrome c, mono- and diheme variants. (140 aa)
AHM61214.1Hypothetical protein. (159 aa)
AHM61230.1COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. (214 aa)
AHM61798.1COG2010 Cytochrome c, mono- and diheme variants. (338 aa)
AHM62184.1COG1143 Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I). (579 aa)
nuoKNAD(P)H-quinone oxidoreductase subunit 4L; 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. (101 aa)
AHM62188.1COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). (584 aa)
AHM62419.1COG3278 Cbb3-type cytochrome oxidase, subunit 1; Belongs to the heme-copper respiratory oxidase family. (737 aa)
AHM62420.1Hypothetical protein. (66 aa)
AHM62421.1COG2010 Cytochrome c, mono- and diheme variants. (296 aa)
AHM62471.1Hypothetical protein. (414 aa)
AHM62473.1COG3256 Nitric oxide reductase large subunit. (754 aa)
AHM62485.1COG2010 Cytochrome c, mono- and diheme variants. (172 aa)
AHM62702.1COG2010 Cytochrome c, mono- and diheme variants. (184 aa)
AHM62705.1Respiratory nitrate reductase, cytochrome c; COG2010 Cytochrome c, mono- and diheme variants. (174 aa)
AHM62708.1Hypothetical protein; COG3278 Cbb3-type cytochrome oxidase, subunit 1. (439 aa)
AHM62815.1Cytochrome c, mono- and diheme variants family protein. (524 aa)
AHM62946.1PKD domain-containing protein; COG3828 Uncharacterized protein conserved in bacteria. (1146 aa)
AHM63030.1Crp/FNR family transcriptional regulator; COG3828 Uncharacterized protein conserved in bacteria. (280 aa)
AHM63059.1COG4654 Cytochrome c551/c552. (131 aa)
AHM63437.1Quinol:cytochrome c oxidoreductase pentaheme cytochrome subunit; COG2010 Cytochrome c, mono- and diheme variants. (161 aa)
AHM63457.1COG1145 Ferredoxin. (115 aa)
AHM63459.1Cytochrome c class I; COG2133 Glucose/sorbosone dehydrogenases. (668 aa)
AHM63630.1Quinol:cytochrome c oxidoreductase pentaheme cytochrome subunit; COG2010 Cytochrome c, mono- and diheme variants. (431 aa)
AHM63633.1COG1511 Predicted membrane protein. (178 aa)
AHM63634.1COG2010 Cytochrome c, mono- and diheme variants. (216 aa)
AHM63636.1Heme/copper-type cytochrome/quinol oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (359 aa)
AHM63637.1COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1; Belongs to the heme-copper respiratory oxidase family. (626 aa)
AHM63640.1COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. (195 aa)
AHM63641.1COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. (252 aa)
Your Current Organism:
Flammeovirgaceae bacterium 311
NCBI taxonomy Id: 1257021
Other names: F. bacterium 311
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